Search: 1000 results found for "PDGF"

Description:

Transforming Growth Factor-Beta 1 Rat Recombinant

Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.

Product # :

CYT-1265

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Description

Transforming Growth Factor-Beta 1 Rat Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa.
TGFB1 Rat 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 TGFB1 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 1 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 1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGP CPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS.
Background
Mouse TGF-β1 as an inducer of EMT [epithelial–mesenchymal transition ] therefore used in in fibrosis, wound healing, cancer invasion, and metastasis. Mouse TGF-β1 decreases E-cadherin expression and increases N-cadherin, vimentin and fibronectin.
TGF-β1 is produced by T regulatory cells (Tregs), Macrophages and monocytes, Platelets, Fibroblasts, Epithelial cells, Endothelial cells, Smooth muscle cells, Tumor cells, Activated immune cells
What is the source or expression system of Mouse TGFB1 Protein?
CHO Cells

What is the Purity of Mouse TGFB1 Protein?
Mouse TGFB1 Protein is >97% pure as determined by SDS-PAGE and SEC-HPLC analyses.

What is the molecular weight of Mouse TGFB1 Protein?
Mouse TGFB1 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Mouse TGFB1 Protein?
The biological functionality of Mouse TGFB1 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Mouse TGFB1 Protein?
The endotoxin level is minimal, Mouse TGFB1 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Mouse TGFB1 Protein?
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASASPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.

Is TGFB1 a homodimer / homodimeric protein?
Yes, TGFB1 is homo dimer consisting of 2 identical chains.

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:

Dickkopf-Related Protein 2 Human Recombinant

Dickkopf 2 homolog (Xenopus laevis), dickkopf related protein-2, hDkk-2.

Product # :

PRO-1205

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Description

DKK2 Human Recombinant produced in E. coli is a single polypeptide chain containing 250 amino acids (34-259) and having a molecular mass of 27.6 kDa.DKK2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The DKK2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Dickkopf-related protein 2 (DKK2) is a member of the dickkopf family, which has a vital role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In adults, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease. DKK2 contains 2 cysteine rich regions and is implicated in embryonic development through its interactions with the Wnt signaling pathway. DKK2 may function as either an agonist or antagonist of Wnt/beta-catenin signaling, depending on the cellular environment and the presence of the co-factor kremen 2. DKK2 protein activity is also controlled by binding to the Wnt co-receptor LRP6 (LDL-receptor related protein 6).
Synonyms
Dickkopf 2 homolog (Xenopus laevis), dickkopf related protein-2, hDkk-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 MGSMKLNSIK SSLGGETPGQ AANRSAGMYQ GLAFGGSKKG KNLGQAYPCS SDKECEVGRY CHSPHQGSSA CMVCRRKKKR CHRDGMCCPS TRCNNGICIP VTESILTPHI PALDGTRHRD RNHGHYSNHD LGWQNLGRPH TKMSHIKGHE GDPCLRSSDC IEGFCCARHF WTKICKPVLH QGEVCTKQRK KGSHGLEIFQ RCDCAKGLSC KVWKDATYSS KARLHVCQKI.

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:

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:

Recombinant Human Anti Vascular Endothelial Growth Factor

Product # :

ANT-601

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Description

Recombinant Human Anti Vascular Endothelial Growth Factor that binds to and inhibits the biologic activity of human VEGF in vitro. Recombinant VEGF Antibody contains human framework regions and the complementarity-determining regions of a murine antibody that binds to VEGF. Recombinant VEGF Antibody is produced in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 149 kDa.

Source

CHO.

Formulation

The protein 25.7mg/ml solution contains 60 mg/ml of a,a-trehalose dihydrate, 5.8 mg/ml of sodium phosphate (monobasic, monohydrate), 1.2 mg/ml of sodium phosphate (dibasic, anhydrous) and 0.4 mg/ml of polysorbate 20, pH-6.

Purity

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

Biological Activity

The ED₅₀ as determined by the proliferation inhibition of HUVEC cell, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 1.1 X 10⁴EU/mg.

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Introduction
Vascular endothelial growth factoris an important signaling proteininvolved in both vasculogenesisand 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 is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Physical Appearance
Clear, colorless solution.
Stability
Recombinant VEGF Antibody should be stored between 2-8°C and should be protected from light. DO NOT FREEZE.
Amino Acid Sequence
LIGHT CHAIN:
DIQMTQSPSS LSASVGDRVT ITCSASQDIS NYLNWYQQKP GKAPKVLIYF TSSLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ YSTVPWTFGQ GTKVEIKRTV AAPSVFIFPP SDEQLKSGTA SVVCLLNNFY PREAKVQWKV DNALQSGNSQ ESVTEQDSKD STYSLSSTLT LSKADYEKHK VYACEVTHQG LSSPVTKSFN
RGEC.

HEAVY CHAIN:
EVQLVESGGG LVQPGGSLRL SCAASGYTFT NYGMNWVRQA PGKGLEWVGW INTYTGEPTY AADFKRRFTF SLDTSKSTAY LQMNSLRAED TAVYYCAKYP HYYGSSHWYF DVWGQGTLVT VSSASTKGPS VFPLAPSSKS TSGGTAALGC LVKDYFPEPV TVSWNSGALT SGVHTFPAVL QSSGLYSLSS VVTVPSSSLG TQTYICNVNH KPSNTKVDKK VEPKSCDKTH TCPPCPAPEL
LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS REEMTKNQVS 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:

Stromal Cell-Derived Factor-1 beta Rat Recombinant (CXCL12)

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

Product # :

CHM-248

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Description

SDF-1 beta Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8.4 kDa. The Rat SDF-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Rat SDF1B protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phsophate buffer pH-7.4 and 0.15M NaCl.

Purity

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

Biological Activity

The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.

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:

Phosphoglucomutase 2 Human Recombinant

Phosphoglucomutase 2, Glucose Phosphomutase 2, Phosphodeoxyribomutase, Phosphopentomutase, EC 5.4.2.2, PGM 2, Phosphoglucomutase-2, EC 5.4.2.7, EC 5.4.2, MSTP006.

Product # :

ENZ-930

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Description

PGM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 635 amino acids (1-612 a.a) and having a molecular mass of 70.7kDa. PGM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PGM2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
PGM2 or Phosphoglucomutase-2 is a protein of the alpha-d-phosphohexomutase family that shares about 20% similarity with mammalian phosphoglucomutase 1. PGM2 Has low glucose 1,6-bisphosphate synthase activity. Furthermore, PGM2 catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. In addition, PGM2 catalyzes the interconversion of glucose-1-phosphate and glucose-6-phosphate.
Synonyms
Phosphoglucomutase 2, Glucose Phosphomutase 2, Phosphodeoxyribomutase, Phosphopentomutase, EC 5.4.2.2, PGM 2, Phosphoglucomutase-2, EC 5.4.2.7, EC 5.4.2, MSTP006.
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 MGSMAAPEGS GLGEDARLDQ ETAQWLRWDK NSLTLEAVKR LIAEGNKEEL RKCFGARMEF GTAGLRAAMG PGISRMNDLT IIQTTQGFCR YLEKQFSDLK QKGIVISFDA RAHPSSGGSS RRFARLAATT FISQGIPVYL FSDITPTPFV PFTVSHLKLC AGIMITASHN PKQDNGYKVY WDNGAQIISP HDKGISQAIE ENLEPWPQAW DDSLIDSSPL LHNPSASINN DYFEDLKKYC FHRSVNRETK VKFVHTSVHG VGHSFVQSAF KAFDLVPPEA VPEQKDPDPE FPTVKYPNPE EGKGVLTLSF ALADKTKARI VLANDPDADR LAVAEKQDSG EWRVFSGNEL GALLGWWLFT SWKEKNQDRS ALKDTYMLSS TVSSKILRAI ALKEGFHFEE TLTGFKWMGN RAKQLIDQGK TVLFAFEEAI GYMCCPFVLD KDGVSAAVIS AELASFLATK NLSLSQQLKA IYVEYGYHIT KASYFICHDQ ETIKKLFENL RNYDGKNNYP KACGKFEISA IRDLTTGYDD SQPDKKAVLP TSKSSQMITF TFANGGVATM RTSGTEPKIK YYAELCAPPG NSDPEQLKKE LNELVSAIEE HFFQPQKYNL QPKAD.

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:

IGF-1 Bovine Recombinant

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

Product # :

CYT-1261

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Description

IGF1 Bovine 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- I is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IGF1 Bovine was lyophilized from a 0.2µm filtered 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 IGF-1 Bovine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution bovine 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 bovine IGF-1 in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

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 Rat

Urogastrone, URG, EGF.

Product # :

CYT-556

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Description

Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Adult Male Rat Submandibular Glands.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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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.
Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.15kDa.

What is the source or expression system of EGF RAT Protein?
Adult Male Rat Submandibular Glands.

What is the Purity of EGF RAT Protein?
EGF RAT Protein is >99% pure as determined by SDS-PAGE.

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

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

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

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

Mouse Anti Human Connective Tissue Growth Factor

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Product # :

ANT-699

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Formulation

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

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CTGF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTGF protein 27-349 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
Clone
PAT18E7AT.
Applications
CTGF antibody has been tested by ELISA, Western blot analysis and ICC/IF 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
CTGF antibody was purified 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:

Epidermal Growth Factor Mouse Recombinant, Biotin

Urogastrone, URG, EGF.

Product # :

CYT-841

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Description

EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) solution contains sterile PBS.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x10⁶units/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 clear solution.
Stability
Should be stored at 4°C.Please do not freeze.
Amino Acid Sequence
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
Background
Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential
Abstract:
This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.
Introduction:
Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.
Protein Engineering and Biotin Conjugation:
EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.
Cellular Signaling Amplification:
The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.
Cellular Assays and Functional Responses:
In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.
Tailored Delivery Strategies:
The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.
Regenerative Medicine and Targeted Therapy:
The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.
Future Prospects and Challenges:
While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.
Conclusion:
In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.
What is the molecular weight/Mw of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein has a total Mw of 7kDa.

What is the source or expression system of MEGF, BIOTIN Protein?
Escherichia Coli.

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

What is the Biological Activity of MEGF, BIOTIN Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.

What is the amino acid sequence of MEGF, BIOTIN Protein?
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.

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

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

Endoglin (27-581) Mouse Recombinant

Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.

Product # :

CYT-972

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Description

Endoglin Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-581 a.a.) and having a molecular mass of 60.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).Endoglin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Endoglin protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.
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
ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 60.9kDa.

What is the source or expression system of CD105 Protein?
Sf9, Baculovirus cells.

What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.

What is the amino acid sequence of CD105 Protein?
ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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:

Growth Hormone Binding Protein Mouse Recombinant

GHR, GHBP, GH receptor, Somatotropin receptor.

Product # :

CYT-1256

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Shipped at Room temp

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Description

Growth Hormone Binding Protein Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids and having a molecular mass of 28 kDa. GHBP Mouse is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Growth Hormone Binding Protein Mouse was lyophilized from a concentrated (1mg/ml) solution with 0.5mg/ml NaHCO3.

Purity

Greater than 95.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

fully biologically active as evidenced by its ability of forming 2:1 complex with human and non-primate GHs.

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Synonyms
GHR, GHBP, GH receptor, Somatotropin receptor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GHBP Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -20C. Upon reconstitution at > 0.1 GHBP Mouse -ECD mg/ml and filter sterilization GHBP can be stored at 4C for several weeks. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GHBP Mouse in sterile 0.4% NaHCO3 adjusted to pH 8 or in distilled water, 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-Phe-Ser-Gly-Ser.
Background
GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon 3 and has been well-characterized. Mutations in GHBP have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short height.

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:

HB-EGF Human Recombinant

HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

Product # :

CYT-119

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 10⁶units/mg.

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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
Synonyms
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-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 Human HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.9kDa.

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

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

What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.

What is the amino acid sequence of HB-EGF Protein?
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.

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

What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-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:

Stromal Cell-Derived Factor-1 alpha Rat Recombinant (CXCL12)

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

Product # :

CHM-354

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Stromal Cell-Derived Factor-1 alpha Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9 kDa. The SDF-1a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CXCL12 protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 150mM NaCl.

Purity

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

Biological Activity

The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

More Info

Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNK.

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 Human Recombinant, His Tag

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-281

Price :

Quantity :

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Shipped with Ice Packs

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Description

Fibroblast Growth Factor -21 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 202 amino acids (29-209) and having a molecular mass of 21.6 kDa (molecular weight on SDS-PAGE will appear higher). The FGF-21 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF-21 His tag protein (1mg/ml) solution in 20mM Tris-HCl buffer pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

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
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
MGSSHHHHHH SSGLVPRGSH MHPIPDSSPL LQFGGQVRQR YLYTDDAQQT EAHLEIREDG TVGGAADQSP ESLLQLKALK PGVIQILGVKTSRFLCQRPD GALYGSLHFD PEACSFRELL LEDGYNVYQS EAHGLPLHLP GNKSPHRDPA PRGPARFLPL PGLPPAPPEP PGILAPQPPD VGSSDPLSMV GPSQGRSPSY AS.
Background
What is the molecular weight/Mw of FGF21,HIS Protein?
FGF21,HIS Protein has a total Mw of 21.6kDa.

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

What is the Purity of FGF21,HIS Protein?
FGF21,HIS Protein is >90% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of FGF21,HIS Protein?
MGSSHHHHHH SSGLVPRGSH MHPIPDSSPL LQFGGQVRQR YLYTDDAQQT EAHLEIREDG TVGGAADQSP ESLLQLKALK PGVIQILGVKTSRFLCQRPD GALYGSLHFD PEACSFRELL LEDGYNVYQS EAHGLPLHLP GNKSPHRDPA PRGPARFLPL PGLPPAPPEP PGILAPQPPD VGSSDPLSMV GPSQGRSPSY AS.

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

What is the endotoxin level for FGF21,HIS Protein?
The endotoxin level is minimal, FGF21,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:

Tumor Necrosis Factor-Alpha Mouse Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-252

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Quantity :

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Shipped at Room temp

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Description

Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

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

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000Units/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-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
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 TNF-a 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:

Keratinocyte Growth Factor-2 Human Recombinant

FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.

Product # :

CYT-303

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Shipped at Room temp

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Description

Keratinocyte Growth Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (40-208) and having a molecular mass of 19300 Dalton. Keratinocyte Growth Factor 2 is highly related to KGF-1(FGF-7), it binds to the same receptor as KGF-1 and shares 57% sequence homology. The FGF10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependant stimulation of FGF receptors by BaF3 indicator cells (measured by ³H-thymidine uptake) is < 0.5 ng/ml, corresponding to a specific activity of 2x10⁶units/mg.

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Introduction
KGF-2 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-10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. Studies of the mouse homolog of suggested that this gene is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of lim bud formation. This gene is also implicated to be a primary factor in the process of wound healing.
Synonyms
FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Keratinocyte Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF10 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-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLGQDMVSPE ATNSSSSSFS SPSSAGRHVR SYNHLQGDVR WRKLFSFTKY FLKIEKNGKV SGTKKENCPY SILEITSVEI GVVAVKAINS NYYLAMNKKG KLYGSKEFNN DCKLKERIEE NGYNTYASFN WQHNGRQMYV ALNGKGAPRR GQKTRRKNTS AHFLPMVVHS.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.79 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 standard solution of FGF-10 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 Recombinant Rhesus Macaque

CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.

Product # :

CYT-1121

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Shipped at Room temp

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Description

Granulocyte Colony Stimulating Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18.9kDa.GCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.

Purity

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

Biological Activity

The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

More Info

Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part 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
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Colony Stimulating Rhesus Macaque 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 Granulocyte Colony Stimulating Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
Background
What is the molecular weight/Mw of GCSF MONKEY Protein?
GCSF MONKEY Protein has a total Mw of 18.9kDa.

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

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

What is the Biological Activity of GCSF MONKEY Protein?
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.

What is the amino acid sequence of GCSF MONKEY Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.

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

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

GDNF Family Receptor Alpha 3 Human Recombinant

GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.

Product # :

CYT-399

Price :

Quantity :

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Shipped with Ice Packs

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sds-page

Description

GFRA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (32-374a.a) and having a molecular mass of 40.7kDa.GFRA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GFRA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.4M urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

sds-page

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Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.
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.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
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN
Background
What is the molecular weight/Mw of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein has a total Mw of 40.7kDa.

What is the source or expression system of GFRA3 HUMAN Protein?
Escherichia Coli.

What is the Purity of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA3 HUMAN Protein?
The biological functionality of GFRA3 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GFRA3 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN

What applications can GFRA3 HUMAN Protein be used in?
GFRA3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA3 HUMAN Protein?
The endotoxin level is minimal, GFRA3 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:

IGF-1 Rat Recombinant

Somatomedin C, IGF-I, IGFIA, IGF1.

Product # :

CYT-289

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IGF-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa. IGF-I is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0ng/ml, corresponding to a specific activity of >500,000units/mg.

More Info

Introduction
The somatomedins, or 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' (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, IGFIA, IGF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFI 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 IGF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGP RGFYFNKPTG YGSSIRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPTKSA.

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

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
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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 Canine Recombinant

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

Product # :

CYT-724

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

GMCSF k9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14.2 kDa. GM-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GMCSF was lyophilized after extensive dialysis against 1xPBS pH 7.4.

Purity

Greater than 96.0% as determined by
1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.

Biological Activity

The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMCSF 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 GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
INFKSFKENL KDFLFNIPFD CWKPVKK.
Background
What is the molecular weight/Mw of GM-CSF K9 Protein?
GM-CSF K9 Protein has a total Mw of 14.2kDa.

What is the source or expression system of GM-CSF K9 Protein?
Escherichia Coli.

What is the Purity of GM-CSF K9 Protein?
GM-CSF K9 Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF K9 Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF1 erythroleukemic cells is typically 1-4 ng/ml.

What is the amino acid sequence of GM-CSF K9 Protein?
APTRSPTLVT RPSQHVDAIQ EALSLLNNSN DVTAVMNKAV KVVSEVFDPE
GPTCLETRLQ LYKEGLQGSL TSLKNPLTMM ANHYKQHCPP TPESPCATQN
INFKSFKENL KDFLFNIPFD CWKPVKK.

What applications can GM-CSF K9 Protein be used in?
GM-CSF K9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF K9 Protein?
The endotoxin level is minimal, GM-CSF K9 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.

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