重组人表皮生长因子/Human EGF 现货
Recombinant Human Epidermal Growth Factor重组人表皮生长因子/Human EGF 现货
Recombinant Human Epidermal Growth Factor重组人表皮生长因子/Human EGF 现货
Recombinant Human Epidermal Growth Factor重组人表皮生长因子/Human EGF 现货
Recombinant Human Epidermal Growth Factor

本公司代理的PrimeGene细胞因子、趋化蛋白、激素、酶、泛素等均有现货销售，货期短，质量保证！

Synonyms

Urogastrone, URG

Synonyms

Synonyms

Urogastrone, URG

Urogastrone, URG

Accession

P01133

Accession

Accession

P01133

P01133P01133

Unigene

Hs.419815.

Unigene

Unigene

Hs.419815.

Hs.419815.Hs.419815.

Source

Escherichia coli.

Source

Source

Escherichia coli.

Escherichia coli.

Molecular Weight

Approximately 6.2 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids.

Molecular Weight

Molecular Weight

Approximately 6.2 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids.

Approximately 6.2 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids.

AA Sequence

NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

AA Sequence

AA Sequence

NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

Purity

> 95 % by SDS-PAGE and HPLC analyses.

Purity

Purity

> 95 % by SDS-PAGE and HPLC analyses.

> 95 % by SDS-PAGE and HPLC analyses.

Biological Activity

Fully biologically active when compared to standard. The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

Biological Activity

Biological Activity

Fully biologically active when compared to standard. The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

Fully biologically active when compared to standard. The ED₅₀50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶6 IU/mg.

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Physical Appearance

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation

Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Formulation

Formulation

Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Endotoxin

Less than 1 EU/μg of rHuEGF as determined by LAL method.

Endotoxin

Endotoxin

Less than 1 EU/μg of rHuEGF as determined by LAL method.

Less than 1 EU/μg of rHuEGF as determined by LAL method.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

Reconstitution

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Stability & Storage

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Usage

This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

Usage

Usage

This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

SDS-PAGE

SDS-PAGE

SDS-PAGE

Reference

1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6.
2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62.
3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58.
4. Cohen S. 2008. J Biol Chem, 283: 33793-7.

Reference

Reference

1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6.
2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62.
3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58.
4. Cohen S. 2008. J Biol Chem, 283: 33793-7.

1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6.
2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62.
3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58.
4. Cohen S. 2008. J Biol Chem, 283: 33793-7.

background

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature human EGF shares 70 % a.a. sequence identity with mature mouse and rat EGF.

background

background

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature human EGF shares 70 % a.a. sequence identity with mature mouse and rat EGF.

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature human EGF shares 70 % a.a. sequence identity with mature mouse and rat EGF.

• 技术参数
• FAQs

技术参数

技术参数技术参数

FAQs

FAQsFAQs

Synonyms

Urogastrone, URG

Synonyms

Synonyms

Urogastrone, URG

Urogastrone, URG

Accession

P01133

Accession

Accession

P01133

P01133P01133

Unigene

Hs.419815.

Unigene

Unigene

Hs.419815.

Hs.419815.Hs.419815.

Source

Escherichia coli.

Source

Source

Escherichia coli.

Escherichia coli.

Molecular Weight

Approximately 6.2 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids.

Molecular Weight

Molecular Weight

Approximately 6.2 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids.

Approximately 6.2 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids.

AA Sequence

NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

AA Sequence

AA Sequence

NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR

Purity

> 95 % by SDS-PAGE and HPLC analyses.

Purity

Purity

> 95 % by SDS-PAGE and HPLC analyses.

> 95 % by SDS-PAGE and HPLC analyses.

Biological Activity

Fully biologically active when compared to standard. The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

Biological Activity

Biological Activity

Fully biologically active when compared to standard. The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶ IU/mg.

Fully biologically active when compared to standard. The ED₅₀50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁶6 IU/mg.

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Physical Appearance

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation

Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Formulation

Formulation

Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Endotoxin

Less than 1 EU/μg of rHuEGF as determined by LAL method.

Endotoxin

Endotoxin

Less than 1 EU/μg of rHuEGF as determined by LAL method.

Less than 1 EU/μg of rHuEGF as determined by LAL method.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

Reconstitution

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Stability & Storage

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Usage

NOT FOR HUMAN USE.

Usage

Usage

NOT FOR HUMAN USE.

NOT FOR HUMAN USE.

SDS-PAGE

SDS-PAGE

SDS-PAGE

Reference

1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6.
2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62.
3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58.
4. Cohen S. 2008. J Biol Chem, 283: 33793-7.

Reference

Reference

1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6.
2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62.
3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58.
4. Cohen S. 2008. J Biol Chem, 283: 33793-7.

1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6.
2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62.
3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58.
4. Cohen S. 2008. J Biol Chem, 283: 33793-7.

background

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature human EGF shares 70 % a.a. sequence identity with mature mouse and rat EGF.

background

background

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature human EGF shares 70 % a.a. sequence identity with mature mouse and rat EGF.

Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and named urogastrone, accordingly. EGF is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature human EGF shares 70 % a.a. sequence identity with mature mouse and rat EGF.