Search: 1000 results found for "placental growth factor"

Description:

Transforming Growth Factor Beta 2 Human Recombinant

Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

Product # :

CYT-441

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Description

TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Prolactin Pegylated Human Recombinant

Mammotropin, Luteotropic hormone, Luteotropin, PRL.

Product # :

CYT-1063

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Description

Prolactin Human Recombinant Pegylated produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids + an additional Ala at n-terminal. Pegylated Prolactin is mono-pegylated having a molecular mass of ~ 39 kDa, however under non-denaturing conditions it behaves as 220 kDa protein due to its increased hydrodynamic volume. The Pegylated Prolactin protein is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3

Purity

Greater than 99.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Human Prolactin was tested for its biological functionality in-vitro by inducing proliferation of Nb2 cells or Baf/3 cells that were stably transfected with Human Prolactin receptors, though its activity is lower than human Prolactin. However, it is anticipated that its biological activity in vivo will be higher than human Prolactin due to prolonged persistence in circulation.

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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Prolactin is secreted when eating, nursing, mating, estrogen treatment and during ovulation. Prolactin's primary role is to promote and maintain lactation but also plays a role in breast cancer development, regulation of reproductive function and immunoregulation.
Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Prolactin in sterile 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-217

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Description

Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x10⁷ IU/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
Background
About EGF:
In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).
Description:
Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.
Function:
By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.
Mechanism:
EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

What is the source or expression system of EGF Protein?
Escherichia Coli.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.

What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.

What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim

Product # :

CYT-1160

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Description

GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (18-144a.a.) and having a molecular mass of 16.6kDa.GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GMCSF protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

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Introduction
The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK
Background
What is the molecular weight/Mw of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein has a total Mw of 16.6kDa.

What is the source or expression system of GM-CSF PORCINE, HIS Protein?
Escherichia Coli.

What is the Purity of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF PORCINE, HIS Protein?
The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.

What is the amino acid sequence of GM-CSF PORCINE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK

What applications can GM-CSF PORCINE, HIS Protein be used in?
GM-CSF PORCINE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF PORCINE, HIS Protein?
The endotoxin level is minimal, GM-CSF PORCINE, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-21 Mouse Recombinant, His Tag

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-516

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Description

Fibroblast Growth Factor -21 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 21.2 kDa. The amino acid sequence of the recombinant human FGF21 is 100% homologous to the amino acid sequence of the Mouse FGF21 without signal sequence and contains 10 a.a. His tag at N-terminal.The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM TRIS, 20mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.
Synonyms
Fibroblast growth factor 21, FGF-21.
Physical Appearance
Filtered white lyophilized powder.
Stability
Lyophilized FGF-21 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture. Add DTT (0.2mM) and NaCl (0.1-0.15M) before freezing to prevent potential aggregation.
Amino Acid Sequence
MKHHHHHHAS AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALKPGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDATSWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY AS.
Background
What is the molecular weight/Mw of FGF21 MOUSE,HIS Protein?
FGF21 MOUSE,HIS Protein has a total Mw of 21.2kDa.

What is the source or expression system of FGF21 MOUSE,HIS Protein?
Escherichia Coli.

What is the Purity of FGF21 MOUSE,HIS Protein?
FGF21 MOUSE,HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF21 MOUSE,HIS Protein?
The biological functionality of FGF21 MOUSE,HIS Protein will be determined in the future.

What is the amino acid sequence of FGF21 MOUSE,HIS Protein?
MKHHHHHHAS AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALKPGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDATSWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY AS.

What applications can FGF21 MOUSE,HIS Protein be used in?
FGF21 MOUSE,HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF21 MOUSE,HIS Protein?
The endotoxin level is minimal, FGF21 MOUSE,HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor 14 Human Recombinant

Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.

Product # :

CYT-756

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Description

FGF14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-247 a.a) and having a molecular mass of 30kDa.FGF14 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

FGF14 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
Fibroblast Growth Factor 14 (FGF14) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in a various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF14 gene mutation is linked with autosomal dominant cerebral ataxia.
Synonyms
Fibroblast growth factor 14, FGF-14, Fibroblast growth factor homologous factor 4, FHF-4, FGF14, FHF4, SCA27, bA397O8.2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.
Background
What is the molecular weight/Mw of FGF14 Protein?
FGF14 Protein has a total Mw of 30kDa.

What is the source or expression system of FGF14 Protein?
Escherichia Coli.

What is the Purity of FGF14 Protein?
FGF14 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF14 Protein?
The biological functionality of FGF14 Protein will be determined in the future.

What is the amino acid sequence of FGF14 Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAAAIA SGLIRQKRQA REQHWDRPSA SRRRSSPSKN RGLCNGNLVD IFSKVRIFGL KKRRLRRQDP QLKGIVTRLY CRQGYYLQMH PDGALDGTKD DSTNSTLFNL IPVGLRVVAI QGVKTGLYIA MNGEGYLYPS ELFTPECKFK ESVFENYYVI YSSMLYRQQE SGRAWFLGLN KEGQAMKGNR VKKTKPAAHF LPKPLEVAMY REPSLHDVGE TVPKPGVTPS KSTSASAIMN GGKPVNKSKT T.

What applications can FGF14 Protein be used in?
FGF14 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF14 Protein?
The endotoxin level is minimal, FGF14 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-9 Rat Recombinant

GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

Product # :

CYT-558

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Quantity :

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Shipped at Room temp

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Description

Rat FGF9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.3kDa.The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF-9 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM NaP, pH-7.5 &, 75mM Ammonium Sulfate.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

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Introduction
Rat and mouse FGF-9 show a very high homology to human FGF-9. The transcripts for FGF-9 have been found in brain and in kidney tissue. Fibroblast Growth Factor-9 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis Fibroblast Growth Factor 9 may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
Synonyms
GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Rat Fibroblast Growth Factor-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF9 Rat Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Rat FGF-9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.
Background
What is the molecular weight/Mw of FGF9 Protein?
FGF9 Protein has a total Mw of 23.3kDa.

What is the source or expression system of FGF9 Protein?
Escherichia Coli.

What is the Purity of FGF9 Protein?
FGF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF9 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

What is the amino acid sequence of FGF9 Protein?
MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.

What applications can FGF9 Protein be used in?
FGF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF9 Protein?
The endotoxin level is minimal, FGF9 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Keratinocye Growth Factor Mouse Recombinant

HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.

Product # :

CYT-721

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Quantity :

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Shipped at Room temp

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Description

Keratinocyte Growth Factor-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18.9 kDa. The FGF-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM Phosphate buffer pH-8 and 0.1M NaCl.

Purity

Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant stimulation of KGF-responsive BaF3 indicator cells (measured by 3H-thymidine uptake) is < 10ng/ml corresponding to a specific activity of 100,000 Units/mg.

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Introduction
KGF is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
Synonyms
HBGF-7, FGF7, FGF-7, KGF, Keratinocyte growth factor, Fibroblast growth factor 7, Heparin-binding growth factor 7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized KGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCNDMSPEQT ATSVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNSYNIMEI RTVAVGIVAI KGVESEYYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHSG GEMFVALNQK GIPVKGKKTK KEQKTAHFLP MAIT.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor (121) Human Recombinant, HEK

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-116

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Description

Recombinant Human VEGF 121 amino acids, produced in HEK cells is a glycosylated 37kDa homodimer and 50kDa homotrimer.The VEGF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

VEGF was lyophilized from a 0.2µm filtered solution containing 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of HUVEC cells (Human Umbilical Vein Endothelial Cells), the ED₅₀ is 3ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized VEGF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Prolactin Pegylated Mouse Recombinant

Product # :

CYT-1247

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Description

Pegylated Prolactin Mouse Recombinant is a single non-glycosilated polypeptide chain having a molecular mass of ~ 39 kDa containing 199 amino acids and an additional Ala at N-terminus Prolactin Mouse was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Mouse Prolactin was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

Purity

Greater than 97.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Mouse Prolactin inhibits proliferation of Nb2 cells or Baf/3 cells stably transfected with human prolactin receptors, though its activity is lower than pegylated human prolactin. However, it is anticipated that its activity in vivo in mice will be higher due to prolonged persistence in circulation.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Prolactin Mouse although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 4 mg/ml and filter sterilization Prolactin mouse can be stored at 4°C for several weeks. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Prolactin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
Prolactin aka as lactotropin and mammotropin, is a neuroendocrine hormone synthesized primarily by the pituitary gland in response to eating but also a variety of other cell types including the placenta, brain and uterus. Prolactin takes part in metabolism, regulation of the immune system and pancreatic development. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.675 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by DNAman computer analysis program of protein sequences.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-5 Human Recombinant

Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.

Product # :

CYT-957

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Description

FGF5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 252 amino acids and having a molecular mass of 27.7kDa.The FGF-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-5 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 100mM sodium chloride pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Fibroblast Growth Factor-5 (FGF5) belongs to the FGF family of mitogenic peptides. In vitro, rhFGF5 is a mitogen for Balb/3T3 fibroblasts and bovine heart endothelial cells. FGF5 is also a major muscle-derived survival factor for cultured spinal motoneurons. In vivo, FGF5 is assumed to play central roles in both embryology and neurobiology. Developmentally, FGF5 mRNA is originally found in the embryoblast followed by the lateral somatic mesoderm, where it may play a part in angiogenesis, as well as the myotomes cranial to the tail region, where it may delay terminal myoblast differentiation during cell migration.
Synonyms
Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-5 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
Background
What is the molecular weight/Mw of FGF5 HUMAN Protein?
FGF5 HUMAN Protein has a total Mw of 27.7kDa.

What is the source or expression system of FGF5 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF5 HUMAN Protein?
FGF5 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF5 HUMAN Protein?
The biological functionality of FGF5 HUMAN Protein will be determined in the future.

What is the amino acid sequence of FGF5 HUMAN Protein?
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
What applications can FGF5 HUMAN Protein be used in?
FGF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF5 HUMAN Protein?
The endotoxin level is minimal, FGF5 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.

Product # :

CYT-221

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Description

Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14477 Dalton. GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GM-CSF was lyophilized after extensive dialysis against 2mM sodium phosphate buffer pH= 7.4±0.1.

Purity

Greater than 98.0% as determined by:
1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.

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Introduction
Granulocyte Macrophage Colony Stimulating Factor (GM-CSF) was first characterized as a growth factor that supports the in-vitro colony formation of granulocytes-macrophages progenitor cells. It is a pleiotropic cytokine and a member of a family of endogenous cytokines of the hematopoietic system. GM-CSF is produced as a response to immune or inflammatory stimuli by activated cells of the hematopoietic system such as T cells, B cells, macrophages, mast cells and also fibroblasts and alveolar epithelial cells. It plays an important role in regulating the proliferation, differentiation, survival and activation of hematopoietic cells such as granulocytes and monocytes ,neutrophiles, basophiles and eosonophoiles, erythroid cells, megakaryocytes and T cells.
Human and mouse GM-CSF have about 56% homology and are species specific. Human GM-CSF is not active on mouse cells and vice versa. It is active on canine and feline cells.
GMCSF is 144 amino acids, 22kDa glycoprotein. It is composed of four bundles alpha helices. Its receptor is heterodimers with a ligand-specific alpha subunit and a betac subunit that is shared with the interleukin IL-3 and IL-5 receptors. This unusual form of receptor assembly likely applies also to IL-3 and IL-5 receptors. Cross-linking the two receptor subunits is required for receptor activation and signaling .
GMCSF has been shown to be involved in maturation, mobilization and antigen presentation of myeloid dentritic cells (DCs) in-vivo or ex-vivo. This function promotes Th1 immune responses, cytotoxcity, anti-angiogenesis as well as allergic inflammation, and the development of autoimmunity. Therefore GMCSF can be used in immunotherapy for the treatment of immune suppressed and immune-compromised patients as well as in veterinary medicine for the same purpose. GM-CSF is also important in regulation of embryo development and pregnancy and specifically in embryo implantation and subsequent development .
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Granulocyte Macrophage Colony Stimulating Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
N-terminal methionine has been completely removed enzymatically.
Background
What is the molecular weight/Mw of GM CSF HUMAN Protein?
GM CSF HUMAN Protein has a total Mw of 14.47kDa.

What is the source or expression system of GM CSF HUMAN Protein?
Escherichia Coli.

What is the Purity of GM CSF HUMAN Protein?
GM CSF HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GM CSF HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.

What is the amino acid sequence of GM CSF HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
N-terminal methionine has been completely removed enzymatically.

What applications can GM CSF HUMAN Protein be used in?
GM CSF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM CSF HUMAN Protein?
The endotoxin level is minimal, GM CSF HUMAN Protein was purified using conventional chromatography techniques.
Protein content
GM-CSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.963 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GEN computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GM-CSF as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Growth Hormone Human Recombinant

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-202

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Description

GH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids and having a molecular mass of 22kDa. Growth Hormone is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GH protein lyophilized from a 0.2µm filtered concentrated solution containing mannitol, and glycine.

Purity

Greater than 96.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by the proliferation assay of rat lymphoma NB2-11 cells and was found to be less than 0.1ng/ml.

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGH should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized HGH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FPTIPLSRLF DNAMLRAHRL HQLAFDTYQE FEEAYIPKEQ KYSFLQNPQT SLCFSESIPT PSNREETQQK SNLELLRISL LLIQSWLEPV QFLRSVFANS LVYGASDSNV YDLLKDLEEG IQTLMGRLED GSPRTGQIFK QTYSKFDTNS HNDDALLKNY GLLYCFRKDM DKVETFLRIV QCRSVEGSCG F.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant, Sf9

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-200

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Description

Vascular Endothelial Growth Factor-121 Human Recombinant produced in insect cells as an 18kDa homodimer, is a glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of approximately 36kDa.VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.The VEGF-121 is purified by proprietary chromatographic techniques.

Source

Sf9, Insect Cells.

Formulation

The protein was lyophilized from a solution containing 50mM acetic acid.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using primary HUVECs. The ED₅₀ for this effect is typically 2-10ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
The lyophilized VEGF121 should be reconstituted in 50mM acetic acid to a concentration not lower than 50µg/ml.
Amino Acid Sequence
APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPS CVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHN KCECRPKKDRARQEKCDKPRR.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor-23 Human Recombinant, His Tag

Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

Product # :

CYT-374

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Description

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain expressed with a -6xHis tag containing a total of 257 amino acids (251 a.a. FGF23+ 6 a.a. His tag) and having a molecular mass of 28629.5 Dalton. The FGF-23 is and purified by chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) was lyophilized from 25mM Tris pH7.5 and 0.6M NaCl solution.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

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Introduction
FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. Mutations FGF23 have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized Fibroblast Growth Factor 23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-23 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.
Background
What is the molecular weight/Mw of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein has a total Mw of 28.6kDa.

What is the source or expression system of FGF23 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF23 HUMAN, HIS Protein?
Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

What is the amino acid sequence of FGF23 HUMAN, HIS Protein?
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.

What applications can FGF23 HUMAN, HIS Protein be used in?
FGF23 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF23 HUMAN, HIS Protein?
The endotoxin level is minimal, FGF23 HUMAN, HIS Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epidermal Growth Factor (Leu-21) Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-466

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Description

EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.
Background
Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications
Abstract:
This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.
Introduction:
Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.
Molecular Insights and Signaling Dynamics:
The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.
Experimental Profiling and Cellular Responses:
In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Prospects:
Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.
Future Challenges and Prospects:
While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).
Conclusion:
In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

What is the source or expression system of EGF Protein?
Escherichia Coli.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.

What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.

What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Endocrine Gland Vascular Endothelial Growth Factor Mouse Recombinant

PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

Product # :

CYT-825

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Quantity :

Shipping Method :

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Description

EG-VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.6kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4 and 3% Trehalose.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
Synonyms
PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.
Background
What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.6kDa.

What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.

What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EG-VEGF Protein?
The biological functionality of EG-VEGF Protein will be determined in the future.

What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Activin-A Human Recombinant, Active

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-145

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Quantity :

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Description

Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 10⁵ units/mg.

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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Insulin-Like Growth Factor 1 Rabbit Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-427

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Insulin-Like Growth Factor-I Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 7639 Dalton.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (0.5mg/ml) solution with 0.02% NaHCO3.

Purity

Greater than 98.0% as determined by:(a) Gel-filtration chromatography under non denaturing conditions.(b) Analysis by SDS-PAGE.

Biological Activity

IGF-I is biologically active when compared to human IGF-1. The ED50, calculated by the dose -dependent proliferation of human MCF/7 cells is 5 to 25ng/ml in the cell culture mixture dependent on culture conditions. Its activity consists of 30-40 % compared to human IGF-1.

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Introduction
The IGFs comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone. Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin'. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A, and somatomedin B. IGF-1 is a small protein secreted mostly but not exclusively by the liver and circulating in blood mostly as a complex with several IGF binding proteins. It has growth-regulating, insulin-like, and mitogenic functions and it is secreted in response to growth hormone stimulation.
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Insulin-Like Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized rbIGF-I in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MTAGPETLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKP

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor 16 Mouse Recombinant

Fibroblast Growth Factor 16, FGF-16, FGF16.

Product # :

CYT-947

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

FGF16 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.8kDa.The FGF-16 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-16 0.2µm filtered solution containing 20mM Tris-HCl, pH 9.0, 1M NaCl, 0.02% Tween-20 and 10% Glycerol.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Fibroblast growth factor 16 (FGF16) is a member of the large FGF family, whose members are heparin-binding growth factors with a core 120 amino acid (a.a.) FGF domain which allows for a common tertiary structure. Human FGF16 cDNA is a 207 aa precursor protein with one N-linked glycosylation site. FGF16 though lacking a typical signal peptide, is efficiently produced by mechanisms other than the classical protein secretion pathway. FGF16 is expressed in cardiac cells and is required for proper heart development. FGF16 gene mutation was also observed in individuals with metacarpal 4-5 fusion. FGF16 has an imperative role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development.
Synonyms
Fibroblast Growth Factor 16, FGF-16, FGF16.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS RDLFRYR.
Background
What is the molecular weight/Mw of FGF16 MOUSE Protein?
FGF16 MOUSE Protein has a total Mw of 23.8kDa.

What is the source or expression system of FGF16 MOUSE Protein?
Escherichia Coli.

What is the Purity of FGF16 MOUSE Protein?
FGF16 MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF16 MOUSE Protein?
The biological functionality of FGF16 MOUSE Protein will be determined in the future.

What is the amino acid sequence of FGF16 MOUSE Protein?
MAEVGGVFAS LDWDLHGFSS SLGNVPLADS PGFLNERLGQ IEGKLQRGSP TDFAHLKGIL RRRQLYCRTG FHLEIFPNGT VHGTRHDHSR FGILEFISLA VGLISIRGVD SGLYLGMNER GELYGSKKLT RECVFREQFE ENWYNTYAST LYKHSDSERQ YYVALNKDGS PREGYRTKRH QKFTHFLPRP VDPSKLPSMS RDLFRYR.

What applications can FGF16 MOUSE Protein be used in?
FGF16 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF16 MOUSE Protein?
The endotoxin level is minimal, FGF16 MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Vascular Endothelial Growth Factor Related Protein Rat Recombinant

VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L.

Product # :

CYT-262

Price :

Quantity :

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Shipped at Room temp

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Description

Vascular Endothelial Growth Factor C Rat Recombinant contains 127 amino acids residues and was fused to a His- tag (6x His) at the C-terminal end. As a result of glycosylation VEGF-C migrates as an 15-20 kDa protein in SDS-PAGE under reducing conditions.

Source

Sf9, Insect Cells.

Formulation

Each mg of VEGF-C Rat contains 50mg BSA and PBS as buffer.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to stimulate phosphorylation of the VEGFR-3/FLT-4 receptor in porcine aortic endothelial cells. The ED50 for this effect is typically 200-300ng/ml corresponding to a Specific Activity of 3,334-5,000IU/mg.

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Introduction
VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. The rat VEGFC cDNA encodes a pre-pro-protein of 416 amino acids residues.
It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant rat VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT -4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant rat VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.
Synonyms
VEGF-C, Vascular endothelial growth factor C, VRP, Flt4 ligand, Flt4-L.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vascular Endothelial Growth Factor-C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-C should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor C in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DTVKLAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGAATNTFFKP PCVSVYRCGGCCNSEGLQCMNTSTGYLSKTLFEITVPLSQGPKPVTISFA NHTSCRCMSKLDVYRQVHSIIHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 3 Human Recombinant, Plant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-588

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Quantity :

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Shipped at Room temp

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Description

TGFB3 Human Recombinant produced in plant is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 118 amino acids and having a molecular mass of 27.2kDa. The TGFB3 is fused to 6xHis tag at N-terminus and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of TGFB3 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 ? 40ng/ml corresponding to a specific activity of 25,000 Units/mg.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TGFB3 in sterile 5mM HCl & 50ug/ml BSA at a concentration of 0.05mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKG
YYANFCSGPCPYLRSADTTHSTVLGLY
NTLNPEASASP
CCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Transforming Growth Factor-Beta 3 Mouse Recombinant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-143

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Description

TGF-β 3 Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.7kDa. The TGF-β 3 is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse TGFB3 protein solution contains 20% Ethanol and 10mM Acetic acid.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the ability to induce chondrogenic differentiation.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered clear solution.
Stability
Mouse TGF-beta 3 although stable at room temperature for 3 weeks, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Amino Acid Sequence
MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Insulin Like Growth Factor-1, Mutant V44M Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-1088

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Quantity :

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Description

IGF1 V44M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7 kDa. The IGF1 V44M is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 V44M Lyophilized from a 0.2 µm filtered concentrated solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that takes part in mammalian growth and development. IGF1 mediates various growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). 3 main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IGF1 V44M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIMDECCFR SCDLRRLEMY.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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