Search: 1000 results found for "HDGF"

Description:

Transforming Growth Factor-Beta 2 Human Recombinant, CHO

Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

Product # :

CYT-1268

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Description

TGFB2 Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Human Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.2 ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.

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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 Transforming Growth Factor-Beta 2 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 Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS.
Background
Recombinant TGFB2 protein is used in cell culture to study extracellular matrix remodelling, tissue regeneration, and developmental biology.
TGFB2 takes part in embryonic development and is involved in fibrosis, wound healing, angiogenesis,

What is the molecular weight / Mw of TGFB2 Protein?
TGFB2 Protein has a total Mw of 25.4kDa.

What is the source or expression system of TGFB2 Protein?
CHO Cells

What is the Purity of TGFB2 Protein?
TGFB2 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of TGFB2 Protein?
Determined by its ability to inhibit the mouse IL4-dependent proliferation of mouse HT2 cells. The expected ED50 for this effect is less than 0.2ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.

What is the amino acid sequence of TGFB2 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS

What applications can TGFB2 Protein be used in?
TGFB2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TGFB2 Protein?
The endotoxin level is minimal, TGFB2 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:

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:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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:

Histone Deacetylase 2, Mouse Anti Human

Histone deacetylase 2, YAF1, HD2, YY1-associated factor 1, transcriptional regulator homolog RPD3, RPD3, EC 3.5.1.98.

Product # :

ANT-742

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
HDAC2 is a member of the histone deacetylase family that performs through the construction of large multiprotein complexes and are in charge of the deacetylation of lysine residues on the N-terminal region of the core histones. HDAC2 forms transcriptional repressor complexes by relating to a diversity of proteins, like YY1- a mammalian zinc-finger transcription factor.
In addition, HDAC2 has a vital part in transcriptional regulation, cell cycle progression and developmental procedures.
Synonyms
Histone deacetylase 2, YAF1, HD2, YY1-associated factor 1, transcriptional regulator homolog RPD3, RPD3, EC 3.5.1.98.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human HDAC2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HDAC2 amino acids 1-488 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT3B1AT.
Applications
HDAC2 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
HDAC2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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-8 Mouse Recombinant, 194 a.a.

FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

Product # :

CYT-840

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Description

FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 5mM Na3PO4 and 50 mM NaCl, pH 7.5.

Purity

Greater than 97.0% as determined by analysis by SDS-PAGE.

Biological Activity

The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF 8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF 8 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 FGF 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR
Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 22.5kDa.

What is the source or expression system of FGF8 Protein?
Escherichia Coli.

What is the Purity of FGF8 Protein?
FGF8 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF8 Protein?
The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

What is the amino acid sequence of FGF8 Protein?
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 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 Receptor 3 Fc Chimera Human Recombinant

Achondroplasia, Thanatophoric Dwarfism, CD333, ACH, CEK2, JTK4, HSFGFR3EX, FGFR3.

Product # :

PKA-232

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Description

Soluble FGFR3 Human recombinant fused using a Xa cleavage site with the Fc part of human IgG1 produced in Fc Chimera is a heterodimeric, glycosylated, Polypeptide chain containing 593aa and having a molecular mass of 170kDa.

Source

Insect Cells.

Formulation

FGFR3 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS.

Purity

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

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Introduction
Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
Synonyms
Achondroplasia, Thanatophoric Dwarfism, CD333, ACH, CEK2, JTK4, HSFGFR3EX, FGFR3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGFR3 although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Upon reconstitution FGFR3 should be stored at 4oC between 2-7 days and for future use below -18oC.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 FGFR-3 in sterile PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ESLGTEQRVV GRAAEVPGPE PGQQEQLVFG SGDAVELSCP PPGGGPMGPT VWVKDGTGLV PSERVLVGPQ RLQVLNASHE DSGAYSCRQR LTQRVLCHFS VRVTDAPSSG DDEDGEDEAE DTGVDTGAPY WTRPERMDKK LLAVPAANTV RFRCPAAGNP TPSISWLKNG REFRGEHRIG GIKLRHQQWS LVMESVVPSD RGNYTCVVEN KFGSIRQTYT LDVLERSPHR PILQAGLPAN QTAVLGSDVE FHCKVYSDAQ PHIQWLKHVE VNGSKVGPDG TPYVTVLKTA GANTTDKELE VLSLHNVTFE DAGEYTCLAG NSIGFSHHSA WLVVLPAEEE LVEADEAGDP RRASIEGRGD PEEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK.

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:

IFN-Gamma Mouse Recombinant

Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-358

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Description

IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.

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

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

What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.

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

What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG 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:

Insulin-Like Growth Factor 1 Human Recombinant, GST Tag

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

Product # :

CYT-690

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Description

IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain fused to a GST tag and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 is supplied in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.

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Introduction
The somatomedins, or insulin-like growth factors (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 (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). Three 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 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. Please avoid freeze thaw cycles.

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:

Hemoglobin-Zeta Human Recombinant

Zeta-globin, HBAZ, HBZ2, Hemoglobin subunit zeta, Hemoglobin zeta chain, HBZ.

Product # :

PRO-803

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Description

HBZ Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 150 amino acids (1-142 a.a.) and having a molecular mass of 16.7 kDa. The HBZ is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HBZ solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Hemoglobin subunit zeta (HBZ) is part of the globin family. Hemoglobin Zeta is alpha-like hemoglobin. The HBZ polypeptide is synthesized in the yolk sac of the early embryo, while alpha-globin is produced throughout fetal and adult life.
Synonyms
Zeta-globin, HBAZ, HBZ2, Hemoglobin subunit zeta, Hemoglobin zeta chain, HBZ.
Physical Appearance
Sterile Filtered clear 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
MSLTKTERTI IVSMWAKIST QADTIGTETL ERLFLSHPQT KTYFPHFDLH PGSAQLRAHG SKVVAAVGDA VKSIDDIGGA LSKLSELHAY ILRVDPVNFK LLSHCLLVTL AARFPADFTA EAHAAWDKFL SVVSSVLTEK YRLEHHHHHH.

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:

IGF-1 Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.

Product # :

CYT-216

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Shipped at Room temp

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Description

IGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.6kDa.IGF-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated solution in PBS, pH 7.0.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.

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Introduction
The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH 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 (IGF2; MIM 147470), and somatomedin B.
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 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 IGF-1 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 TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Background
IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of:
● Two cell-surface receptors (IGF1R and IGF2R)
● Two ligands (IGF-1 and IGF-2)
● A family of six high-affinity IGF-binding proteins.
● Proteases.
The Effect IGF Has On The Body
Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body.
Diseases And IGF
Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies.
It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS.
How Was IGF Discovered?
Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor.
What’s The Difference Between IGF-1 And IGF-2?
The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells.
The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.
What is the molecular weight/Mw of IGF1 HUMAN Protein?
IGF1 HUMAN Protein has a total Mw of 7.6kDa.

What is the source or expression system of IGF1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IGF1 HUMAN Protein?
IGF1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 HUMAN Protein?
The biological activity was determined by the cell proliferation assay using serum free human MCF-7 cells in <2ng/ml, corresponding to a Specific Activity of >5.0 x 105IU/mg.
What is the amino acid sequence of IGF1 HUMAN Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

What applications can IGF1 HUMAN Protein be used in?
IGF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 HUMAN Protein?
The endotoxin level is minimal, IGF1 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:

Decorin Human Recombinant, Sf9

Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.

Product # :

PRO-2232

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Description

DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 335 amino acids (31-359a.a.) and having a molecular mass of 37.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). DCN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

DCN protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
Synonyms
Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.
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
DEASGIGPEV PDDRDFEPSL GPVCPFRCQC HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS LKGLNNLAKL GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYKH HHHHH.

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-18 Human Recombinant

Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

Product # :

CYT-120

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Description

FGF-18 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 21.1kDa. The FGF-18 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-18 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×10⁶ units/mg.

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Introduction
Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.
Synonyms
Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF-18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-18 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 FGF-18 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AEENVDFRIH VENQTRARDD VSRKQLRLYQ LYSRTSGKHI QVLGRRISAR GEDGDKYAQL LVETDTFGSQ VRIKGKETEF YLCMNRKGKL VGKPDGTSKE CVFIEKVLEN NYTALMSAKY SGWYVGFTKK GRPRKGPKTR ENQQDVHFMK RYPKGQPELQ KPFKYTTVTK RSRRIRPTHP A.
Background
What is the molecular weight/Mw of FGF18 Protein?
FGF18 Protein has a total Mw of 21.1kDa.

What is the source or expression system of FGF18 Protein?
Escherichia Coli.

What is the Purity of FGF18 Protein?
FGF18 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF18 Protein?
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

What is the amino acid sequence of FGF18 Protein?
AEENVDFRIH VENQTRARDD VSRKQLRLYQ LYSRTSGKHI QVLGRRISAR GEDGDKYAQL LVETDTFGSQ VRIKGKETEF YLCMNRKGKL VGKPDGTSKE CVFIEKVLEN NYTALMSAKY SGWYVGFTKK GRPRKGPKTR ENQQDVHFMK RYPKGQPELQ KPFKYTTVTK RSRRIRPTHP A.

What applications can FGF18 Protein be used in?
FGF18 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF18 Protein?
The endotoxin level is minimal, FGF18 Protein was purified using conventional chromatography tech

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 13 Human Recombinant

Fibroblast growth factor 13, FGF-13, Fibroblast growth factor homologous factor 2, FHF-2, FGF13, FHF2.

Product # :

CYT-121

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Quantity :

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Shipped at Room temp

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Description

FGF13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.6kDa.The FGF-13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF13 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 0.5M NaCl, pH 7.4.

Purity

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

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Introduction
Fibroblast growth factor 13 (FGF-13) is a member of the large FGF family which has at least 23 members. Most of its members are binding growth factors with a core 120 amino acid (aa) FGF domain which allows for a mutual tertiary structure. Human and mouse FGF13 are 245 aa proteins which arise from genes that show N-terminal alternative splicing. Transcripts for 245 aa, 199 aa, 226 aa, 192 aa and 255 aa have been identified in human and mouse, with almost complete cross-species aa identity among all splice forms (greater than 98%). FGF13 is identified in the fetal ependyma, dorsal root and cranial ganglia, both atrial and ventricular myocardium, and in renal collecting duct-associated mesenchyme.
Synonyms
Fibroblast growth factor 13, FGF-13, Fibroblast growth factor homologous factor 2, FHF-2, FGF13, FHF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-13 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 FGF-13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST.
Background
What is the molecular weight/Mw of FGF13 Protein?
FGF13 Protein has a total Mw of 27.6kDa.

What is the source or expression system of FGF13 Protein?
Escherichia Coli.

What is the Purity of FGF13 Protein?
FGF13 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF13 Protein?
The biological functionality of FGF13 Protein will be determined in the future.

What is the amino acid sequence of FGF13 Protein?
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST.

What applications can FGF13 Protein be used in?
FGF13 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF13 Protein?
The endotoxin level is minimal, FGF13 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 17 Human Recombinant

Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

Product # :

CYT-817

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Description

FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa.

Source

Escherichia Coli.

Formulation

FGF17 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

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 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

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Introduction
Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.
Synonyms
Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF17 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 FGF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.
Background
What is the molecular weight/Mw of FGF17 Protein?
FGF17 Protein has a total Mw of 22.6kDa.

What is the source or expression system of FGF17 Protein?
Escherichia Coli.

What is the Purity of FGF17 Protein?
FGF17 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF17 Protein?
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 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

What is the amino acid sequence of FGF17 Protein?
MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

What applications can FGF17 Protein be used in?
FGF17 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF17 Protein?
The endotoxin level is minimal, FGF17 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:

Kruppel-Like Factor 4 Human Recombinant, His Tag

Kruppel-Like Factor 4 (Gut), GKLF, EZF, Epithelial Zinc Finger Protein EZF, Gut-Enriched Krueppel-Like Factor, Endothelial Kruppel-Like Zinc Finger Protein, Krueppel-Like Factor 4, Krueppel-like factor 4, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor.

Product # :

PRO-2186

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Description

KLF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (11-395 a.a) and having a molecular mass of 44.2kDa. KLF4 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

KLF4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.
Synonyms
Kruppel-Like Factor 4 (Gut), GKLF, EZF, Epithelial Zinc Finger Protein EZF, Gut-Enriched Krueppel-Like Factor, Endothelial Kruppel-Like Zinc Finger Protein, Krueppel-Like Factor 4, Krueppel-like factor 4, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAVS DALLPSFSTF ASGPAGREKT LRQAGAPNNR WREELSHMKR LPPVLPGRPY DLAAATVATD LESGGAGAAC GGSNLAPLPR RETEEFNDLL DLDFILSNSL THPPESVAAT VSSSASASSS SSPSSSGPAS APSTCSFTYP IRAGNDPGVA PGGTGGGLLY GRESAPPPTA PFNLADINDV SPSGGFVAEL LRPELDPVYI PPQQPQPPGG GLMGKFVLKA SLSAPGSEYG SPSVISVSKG SPDGSHPVVV APYNGGPPRT CPKIKQEAVS SCTHLGAGPP LSNGHRPAAH DFPLGRQLPS RTTPTLGLEE VLSSRDCHPA LPLPPGFHPH PGPNYPSFLP DQMQPQVPPL HYQELMPPGS CMPEEPKPKR GRRSWPRKRT AT.

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, HEK

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

Product # :

CYT-091

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Shipped at Room temp

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Description

Growth Hormone Human Recombinant produced in HEK cells is a non-glycosylated monomer, having a total molecular weight of 22kDa.The GH is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The GH was lyophilized from 1.13mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The activity was determined by the dose dependent stimulation of the proliferation of rat lymphoma line Nb2-11 cells (prolactin indicator cell line), the ED₅₀ is 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 GH 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 GH in sterile 1xPBS 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:

Recombinant Human Heparanase-1 Active

Product # :

ENZ-1032

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Description

Heparanase Active Enzyme is produced in CHO cells.The protein is purified by several orthogonal chromatography steps.

Formulation

Heparanase Active Enzyme is supplied in20mM Acetate buffer and 750mM NaCl pH 5.4.

Purity

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

Biological Activity

The specific activity of Heparanase Active Enzyme in-house standard is about 0.7 Units (1 unit = 1 μmole of reducing ends of heparan sulfate substrate formed per minute per mg Heparanase Active Enzyme at 37°C). The enzymatic activity of each Heparanase Active Enzyme batch is comparable to the standard as determined by activity assay in which immobilized heparan, released due to heparanase activity, is quantified colorimetrically. Recommended reaction buffer: 20 mM Citrate Phosphate buffer, pH 5.4; 50mM NaCl; 1mM CaCl2.

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Introduction
Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes (1,2,3). Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis (4,5). Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form (1,6). Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival (7,8).
Data Sheet
To view the FULL VERSION data sheet click Heparanase-1 Active Enzyme
Specificity
Heparanase Active Enzyme is identified by Western blot analysis with polyclonalrabbit anti-HPA1 antibodies as 2 subunits of 8-kDa and 50-kDa.
Shipping Conditions
Heparanase Active Enzyme is shipped frozen on dry ice unless stated otherwise by the customer. Shipping fees to N. America and W. Europe is $400 Shipping fees to Asia, Australia and E. Europe is $500
Storage Procedures
Store at –80ºC, avoid repeated freeze-thaw cycles.

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:

Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant HEK

C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

Product # :

PRO-1639

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Description

SERPING1 Human Recombinant produced by transfected human cells is a single polypeptide chain containing 486 amino acids (23-500). SERPING1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

SERPING1 was lyophilized from a 0.2 µM filtered solution of 20mM Tris-HCl and 150mM NaCl, pH 8.0.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.
Synonyms
C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SERPING1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPING1 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 SERPING1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTT
EPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKK
VETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAI
RDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTT
FDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQ
ALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQ
HQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFMLWDQQHKFPVFMGRVYDPRAVDHHHHHH

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:

Interferon Induced With Helicase C Domain 1 Human Recombinant

Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

Product # :

PRO-1505

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Description

IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 Insect Cells.

Formulation

IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

Purity

Greater than 93.0% as determined by SDS-PAGE.

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Introduction
IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.
Synonyms
Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.
Physical Appearance
Sterile Filtered 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. Avoid multiple freeze-thaw cycles.

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:

NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 4 Human Recombinant

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4, Hormone-regulated proliferation-associated protein of 20 kDa, NDUFAF4, C6orf66, HRPAP20, HSPC125, My013, bA22L21.1.

Product # :

ENZ-658

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Description

NDUFAF4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1-175) and having a molecular mass of 22.7kDa.NDUFAF4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NDUFAF4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (NDUFAF4) is involved in the compilation of mitochondrial NADH: ubiquinone oxidoreductase complex (complex I). In addition, NDUFAF4 is involved in cell proliferation and survival of hormone-dependent tumor cells. NDUFAF4 may also be a regulator of breast tumor cell invasion. NDUFAF4 gene mutations cause the mitochondrial complex I deficiency.
Synonyms
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4, Hormone-regulated proliferation-associated protein of 20 kDa, NDUFAF4, C6orf66, HRPAP20, HSPC125, My013, bA22L21.1.
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 MGSMGALVIR GIRNFNLENR AEREISKMKP SVAPRHPSTN SLLREQISLY PEVKGEIARK DEKLLSFLKD VYVDSKDPVS SLQVKAAETC QEPKEFRLPK DHHFDMINIK SIPKGKISIV EALTLLNNHK LFPETWTAEK IMQEYQLEQK DVNSLLKYFV TFEVEIFPPE DKKAIRSK.

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:

Biglycan Human Recombinant, Sf9

BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

Product # :

PRO-2536

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Description

BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

The BGN solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 for this effect is ≤ 20 ug/ml. The specific activity is measured by inhibiting the cell growth using 3T3‑ L1 mouse embryonic fibroblast adipose-like cells.

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Introduction
Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.
Synonyms
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
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
ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.

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:

Neuregulin-1/Heregulin-b1 Human Recombinant

Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.

Product # :

CYT-733

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Description

Recombinant Human Neuregulin-1/Heregulin-b1 produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 177-241) containing 65 amino acids and having a total molecular mass of 7.5kDa. NRG1-B1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 1×PBS, pH 7.4 and 5% trehalose.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 0.5ng/ml, corresponding to a specific activity of >2.0×10⁶ units/mg.

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Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. HRG1-b1 is comprised of an Ig domain and an EGF-like domain which is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. Even though HRG1-b1 biological effects are still unclear, it has been discovered to advance motility and invasiveness of breast cancer cells which in addition might entail up-regulation of expression and function of the autocrine motility-promoting factor (AMF).
Synonyms
Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NRG1-B1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-B1 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 NRG1-B1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE.

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:

Heat Shock Transcription Factor-1, Mouse Anti Human

HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.

Product # :

ANT-328

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Formulation

1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% Glycerol.

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Introduction
The transcription of heat-shock genes is rapidly induced after temperature stress in response to environmental changes, and it is also involved in oogenesis, spermatogenesis, and placental development. Hsp90, is a major repressor of HSF1 gene. HSF1 is known for its participation in heat shock response. HSF1 protein regulates the transcription of hundreds of targets, such as genes involved in protein folding, detoxification, energy generation, carbohydrate metabolism, and cell wall organization. HSF1 binds to MTA1 in vitro & in breast carcinoma. Suppression of estrogen-dependent transcription may contribute to role of HSF1 in cancer. Human cancer lines of diverse origins express higher dependence on HSF1 function to maintain proliferation and survival than their non-transformed counterparts. HSF1 induces anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease. HSF1 is directly involved in the regulation of HO1 havi
Synonyms
HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.
Immunogen
Anti-human HSF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSF1 amino acids 1-529 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PJ7F9AT.
Applications
HSF1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000~ 2,000. Recommended starting dilution is 1:1,000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
HSF1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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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