Search: 1000 results found for "stem cell factor"

Description:

Proheparin-Binding EGF-like Growth Factor Human Recombinant, His Tag

Proheparin-binding EGF-like growth factor, HBEGF, DTR, DTS, HEGFL, HB-EGF, Heparin-binding EGF-like growth factor, Diphtheria toxin receptor, DT-R, DTSF.

Product # :

CYT-761

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

HB-EGF His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (63-148) and having a molecular mass of 12.1kDa.HB-EGF His is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HB-EGF His solution (0. 5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

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 heparin and heparin 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
Proheparin-binding EGF-like growth factor, HBEGF, DTR, DTS, HEGFL, HB-EGF, Heparin-binding EGF-like growth factor, Diphtheria toxin receptor, DT-R, DTSF.
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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDLQEADL DLLRVTLSSK PQALATPNKE EHGKRKKKGK GLGKKRDPCL RKYKDFCIHG ECKYVKELRA PSCICHPGYH GERCHGLSL.
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 12.1kDa.

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 >85% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of HB-EGF Protein?
MGSSHHHHHH SSGLVPRGSH MGSDLQEADL DLLRVTLSSK PQALATPNKE EHGKRKKKGK GLGKKRDPCL RKYKDFCIHG ECKYVKELRA PSCICHPGYH GERCHGLSL.

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:

Tumor Necrosis Factor Receptor 2 Fusion Protein Human Recombinant

Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

Product # :

CYT-422

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Recombinant Human Tumor Necrosis Factor Receptor 2 Fusion Protein produced in CHO is a dimeric, glycosylated, polypeptide chain consisting of the extracellular ligand-binding portion of the human 75 kilo Dalton (p75) tumor necrosis factor receptor 2 (TNFR2) linked to the Fc portion of human IgG1. The Fc component of TNFR2 contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. It consists of 934 amino acids and has an apparent molecular weight of approximately 150 kilo Daltons.The TNFR2 is purified by standard chromatographic techniques.

Source

Chinese Hamster Ovarian Cells (CHO).

Formulation

Each mg contains 1.6mg mannitol, 0.4 mg sucrose and 48 µg tromethamine.

Purity

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

Biological Activity

Potency is determined by its ability to neutralize TNF-alpha mediated growth inhibition of A375 cells, corresponding to a Specific Activity of 17,000,000 IU/mg.

More Info

Introduction
TNFR binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. It plays an important role in the inflammatory processes of rheumatoid arthritis (RA), polyarticular-course juvenile rheumatoid arthritis (JRA), and ankylosing spondylitis and the resulting joint pathology. In addition, TNF plays a role in the inflammatory process of plaque psoriasis. Elevated levels of TNF are found in involved tissues and fluids of patients with RA, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75), exist naturally as monomeric molecules on cell surfaces and in soluble forms. Biological activity of TNF is dependent upon binding to either cell surface TNFR. Recombinant Human TNFR is a dimeric soluble form of the p75 TNF receptor that can bind to two TNF molecules.
It inhibits the activity of TNF in vitro and has been shown to affect several animal models of inflammation, including murine collagen-induced arthritis. TNFR inhibits binding of both TNF? and TNF? (lymphotoxin alpha [LT?]) to cell surface TNFRs, rendering TNF biologically inactive. Cells expressing transmembrane TNF that bind to TNFR are not lysed in vitro in the presence or absence of complement.
TNFR can also modulate biological responses that are induced or regulated by TNF, including expression of adhesion molecules responsible for leukocyte migration (i.e., E-selectin and to a lesser extent intercellular adhesion molecule-1 [ICAM-1]), serum levels of cytokines (e.g., IL-6), and serum levels of matrix metalloproteinase-3 (MMP-3 or stromelysin).
Synonyms
Tumor necrosis factor receptor superfamily member 1B,Tumor necrosis factor receptor 2, TNF-R2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b antigen, Etanercept, TBPII, TNFBR, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor Receptor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFR2 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 TNFR2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Osteoclast Stimulating Factor-1, Mouse Anti Human

SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

Product # :

ANT-056

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info

Formulation

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

More Info

Introduction
OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.
Synonyms
SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.
Immunogen
Anti-human OSTF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human OSTF1 amino acids 1-217 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT9G4AT.
Applications
OSTF1 antibody has been tested by ELISA, Western blot analysis, Flow cytometry 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
OSTF1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Epidermal Growth Factor Mouse Recombinant, His Tag

Urogastrone, URG, EGF.

Product # :

CYT-138

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
SDS-PAGE

Description

EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids (977-1029) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGF solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

More Info

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 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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
Background
Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects
Abstract:
This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications.
Protein Engineering and His Tag Integration:
The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag.
Chromatographic Purification and His Tag Affinity:
Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product.
Structural and Functional Insights:
The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions.
Cellular Assays and Bioactivity Assessment:
In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses.
Therapeutic Prospects and Targeted Delivery:
The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells.
Future Directions and Challenges:
While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity.
Conclusion:
In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and precision medicine.
What is the molecular weight/Mw of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein has a total Mw of 8.6kDa.

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

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

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

What is the amino acid sequence of EGF MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

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

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

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

Description:

POU Class 5 Homeobox 1 Human Recombinant

POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.

Product # :

PRO-088

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

POU5F1 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-265) and having a molecular mass of 32.2 kDa.POU5F1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The POU5F1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.
Synonyms
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
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 MHFYRLFLGA TRRFLNPEWK GEIDNWCVYV LTSLLPFKIQ SQDIKALQKE LEQFAKLLKQ KRITLGYTQA DVGLTLGVLF GKVFSQTTIC RFEALQLSFK NMCKLRPLLQ KWVEEADNNE NLQEICKAET LVQARKRKRT SIENRVRGNL ENLFLQCPKP TLQQISHIAQ QLGLEKDVVR VWFCNRRQKG KRSSSDYAQR EDFEAAGSPF SGGPVSFPLA PGPHFGTPGY GSPHFTALYS SVPFPEGEAF PPVSVTTLGS PMHSN.

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:

Neurotrophin-3 Mouse Recombinant

Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

Product # :

CYT-688

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Neurotrophin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids and having a molecular mass of 13.6kDa. The NT-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 0.02% TFA.

Purity

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

Biological Activity

The activity, as determined by the dose-dependent proliferation of BaF3 cells transfected with the TrkB receptor, is typically in the range of 1-10 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

More Info

Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
YAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

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 Receptor Type 2 Human Recombinant, Sf9

Tumor Necrosis Factor Receptor Superfamily, Member 1B, TNFR2, TNFBR, Tumor Necrosis Factor Receptor Type II, Tumor Necrosis Factor Receptor 2, P80 TNF-Alpha Receptor, TNF-RII, TNF-R2, P75, Tumor Necrosis Factor Receptor Superfamily Member 1B, Tumor Necrosis Factor Binding Protein 2, Tumor Necrosis Factor Beta Receptor, Soluble TNFR1B Variant 1, P75 TNF Receptor, CD120b Antigen, Etanercept, TNF-R-II, TNF-R75, P75TNFR, TNFR-II, CD120b, TNFR1B, TNFR80, TBPII.

Product # :

CYT-908

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

TNFR2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (23-257 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 241 amino acids and having a molecular mass of 25.9kDa. TNFR2 is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFR2 protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 0.2 μg/ml and is measured by its ability to inhibit cytotoxicity using L-929 mouse fibroblast cells in the presence of Human TNF-α.

More Info

Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
Synonyms
Tumor Necrosis Factor Receptor Superfamily, Member 1B, TNFR2, TNFBR, Tumor Necrosis Factor Receptor Type II, Tumor Necrosis Factor Receptor 2, P80 TNF-Alpha Receptor, TNF-RII, TNF-R2, P75, Tumor Necrosis Factor Receptor Superfamily Member 1B, Tumor Necrosis Factor Binding Protein 2, Tumor Necrosis Factor Beta Receptor, Soluble TNFR1B Variant 1, P75 TNF Receptor, CD120b Antigen, Etanercept, TNF-R-II, TNF-R75, P75TNFR, TNFR-II, CD120b, TNFR1B, TNFR80, TBPII.
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
LPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPTRSMAPG AVHLPQPVST RSQHTQPTPE PSTAPSTSFL LPMGPSPPAE GSTGDHHHHH H

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

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

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.

More Info

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:

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 :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
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

More Info

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:

LR3 Insulin Like Growth Factor-1 Human Recombinant

R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.

Product # :

CYT-022

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
sds-page

Description

The LR3 is a long-term analog of human IGF-1, specifically designed and manufactured for mammalian cell culture to support large-scale manufacturing of recombinant biopharmaceuticals. Recombinant Human LR3 Insulin Like Growth Factor-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9.1kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.2.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the stimulation of protein synthesis in L6 myoblasts is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.

sds-page

More Info

Introduction
IGF-1 (Insulin-like growth factor-1) is a major hormonal mediator of statural growth. Under regular circumstances, GH (growth hormone) binds to its receptor in the liver, and other tissues, and stimulates the synthesis/secretion of IGF-1. In target tissues, the Type 1 IGF receptor, that is homologous to the insulin receptor, is activated by IGF-1, leading to intracellular signaling which stimulates multiple processes leading to statural growth. IGF-1 metabolic actions are partly directed at stimulating the uptake of glucose, fatty acids, and amino acids so that metabolism supports growing tissues.
Synonyms
R3 IGF1, R3 IGF-1, R3IGF1, R3IGF-1, LONG IGF1, LONG IGF-1, LONG R3 IGF1, LONG R3IGF1, LONG R3 IGF-1, LONG R3IGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LR3 IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution the LR3 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 LR3 IGF1 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIV DECCFRSCDLRRLEMYCAPLKPAKSA.

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:

TRAIL / APO2 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

Product # :

CYT-443

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.

Purity

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

Biological Activity

The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED₅₀ for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.

More Info

Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.

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

Description:

Vascular Endothelial Growth Factor Rat Recombinant, His Tag

VEGF-A, Vascular permeability factor, VPF, VEGF.

Product # :

CYT-854

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

VEGF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (206-325 a.a) and having a molecular mass of 16.7kDa.VEGF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VEGF protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 50% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
VEGF-A, Vascular permeability factor, VPF, VEGF.
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 MGSHMAPTTE GEQKAHEVVK FMDVYQRSYC RPIETLVDIF QEYPDEIEYI FKPSCVPLMR CAGCCNDEAL ECVPTSESNV TMQIMRIKPH QSQHIGEMSF LQHSRCECRP KKDRTKPEKC DKPRR

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:

Platelet-Derived Growth Factor AA Rat Recombinant

Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.

Product # :

CYT-776

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Platelet-derived Growth Factor AA Human Recombinant is a disulfide-linked homodimer Consists of two A chains containing 111 amino acids each and having a total molecular mass of 25.3KDa. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PDGF-AA was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.0.

Purity

Greater than 97.0% 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 Balb/c 3T3 cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 10⁵ IU/mg.

More Info

Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF
have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-derived Growth Factor AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 Platelet-derived Growth Factor-AA in Sterile 4mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
MSIEEAIPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATSNLN PDHREEETDV R.

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:

Bone Marrow Stromal Cell Antigen 2 Human Recombinant

Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin, NPC-A-7.

Product # :

CYT-059

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page

Description

BST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (50-161) and having a molecular mass of 14.8 kDa.The BST2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BST2 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
BST2 takes part in the growth and development of B-cells. The human cellular protein BST2 inhibits retrovirus infection by maintaining the diffusion of virus particles after budding from infected cells. BST2 was originally discovered as an inhibitor to HIV-1 infection in the absence of Vpu, but it is also known to inhibit the release of other viruses such as the Lassa and Marburg virions. In addition, BST2 has a part in B-cell activation in rheumatoid arthritis.
Synonyms
Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin,
NPC-A-7.
Physical Appearance
BST2 is supplied as a 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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS
Background
The Impact of Bone Marrow Stromal Cell Antigen 2 Human Recombinant in Regenerative Medicine
Introduction
As regenerative medicine progresses from the realm of imagination to tangible reality, Bone Marrow Stromal Cell Antigen 2 (BST-2) human recombinant surfaces as a noteworthy contributor with the potential to reshape the future of therapeutic practices.
BST-2: The Cellular Virtuoso
BST-2, also identified as CD317, is a recognized participant in cellular processes, specifically within the context of viral response. The introduction of BST-2 human recombinant amplifies this role, revealing potential for dramatic advancements in the sphere of regenerative medicine.
Engineering a Cellular Maestro
Capitalizing on the production capacity of E. coli, we successfully synthesized BST-2 human recombinant. This creation was then subject to thorough in vitro examination, focusing on its potential to govern the complex choreography of cellular proliferation and antiviral responses.
Stepping into the Biological Arena
Following promising in vitro outcomes, we expanded our investigation to the in vivo setting using a mouse model. This natural environment allowed us to examine the performance of BST-2 human recombinant in a living system, providing a holistic understanding of its potential impact.
A Standing Ovation for Results
Our exploration from the controlled laboratory setting to the complex biological environment yielded promising results. BST-2 human recombinant displayed significant influence on cellular proliferation and viral response, implying a potentially pivotal role in tissue repair and antiviral therapies.
Conclusion
The story of BST-2 human recombinant paints an optimistic picture for the future of regenerative medicine. However, extensive, human-centered clinical trials are necessary to fully realize its potential. As we continue to explore this riveting narrative, we stand on the brink of a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST2 Protein?
BST2 Protein has a total Mw of 14.8kDa.

What is the source or expression system of BST2 Protein?
Escherichia Coli.

What is the Purity of BST2 Protein?
BST2 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of BST2 Protein?
The biological functionality of BST2 Protein will be determined in the future.

What is the amino acid sequence of BST2 Protein?
MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS

What applications can BST2 Protein be used in?
BST2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BST2 Protein?
The endotoxin level is minimal, BST2 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:

Bone Marrow Stromal Cell Antigen 1 Human Recombinant

Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

Product # :

CYT-1071

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.
Synonyms
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 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
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
Background
The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine
Introduction
In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.
BST-1: A Versatile Player
BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.
Engineering a Cellular Conductor
With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.
Entering the Biological Stage
Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.
An Enthusiastic Applause for Results
Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.
Conclusion
The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST1 Protein?
BST1 Protein has a total Mw of 30.5kDa.

What is the source or expression system of BST1 Protein?
Sf9, Baculovirus cells.

What is the Purity of BST1 Protein?
BST1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BST1 Protein?
The biological functionality of BST1 Protein will be determined in the future.

What is the amino acid sequence of BST1 Protein?
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

What applications can BST1 Protein be used in?
BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BST1 Protein?
The endotoxin level is minimal, BST1 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:

Serine/arginine-Rich Splicing Factor 1 Human Recombinant, Sf9

SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.

Product # :

PRO-2417

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

SRSF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (1-248) and having a molecular mass of 28.5kDa. SRSF1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SRSF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 100mM KCl, 1mM DTT, 0.2mM EDTA and 40% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Serine/arginine-rich splicing factor 1 (SFRS1) belongs to the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. SFRS1 binds to pre-mRNA transcripts and components of the spliceosome, and can either initiate or inhibit splicing depending on the position of the pre-mRNA binding site. The ability of SFRS1 to activate splicing is controlled by phosphorylation and interactions with other splicing factor associated proteins.
Synonyms
SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 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
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRTHH HHHH.

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:

beta Nerve Growth Factor Human Recombinant, HEK

Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

Product # :

CYT-079

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.

Source

HEK293 cells.

Formulation

The b-NGF was lyophilized from 1mg/ml in 20mM PB and 0.25M NaCl pH-7.5.

Purity

Greater than 97% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED₅₀ is <0.04-0.4ng/ml.

More Info

Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized b-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution b-NGF 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 b-NGF in sterile distilled pyrogen free water at a concentration of 0.25mg/ml.
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.

What is the source or expression system of B NGF Protein?
HEK293 cells.

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

What is the Biological Activity of B NGF Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.

What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.

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

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

CD70 Human Recombinant

CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.

Product # :

CYT-880

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

TNFSF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (39-193 a.a) and having a molecular mass of 19.5kDa. TNFSF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFSF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

More Info

Introduction
CD70 also known as TNFSF7 is a cytokine which binds to CD27. TNFSF7 takes part in T-cell activation as well as induces the proliferation of costimulated T-cells. Moreover, TNFSF7 enhances the generation of cytolytic T-cells. Among the diseases which are associated with TNFSF7: Include acute myocarditis & Myocarditis.
Synonyms
CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.
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 MGSQRFAQAQ QQLPLESLGW DVAELQLNHT GPQQDPRLYW QGGPALGRSF LHGPELDKGQ LRIHRDGIYM VHIQVTLAIC SSTTASRHHP TTLAVGICSP ASRSISLLRL SFHQGCTIAS QRLTPLARGD TLCTNLTGTL LPSRNTDETF FGVQWVRP.

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:

Platelet-Derived Growth Factor B Human Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

Product # :

CYT-492

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

PDGF-B Human Recombinant mature chain produced in E.Coli is a non-glycosylated, polypeptide chain containing 109 amino acids fragment (82-190) and having a molecular mass of 16.75 kDa. The PDGF-B is fused with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Platelet-Derived Growth Factor-B is supplied in 25mM Na-Acetate pH 4.8, 1mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
The term ‘PDGF’ refers to a family of disulphide bond-linked dimeric isoforms that act as autocrine and paracrine growth factors and are produced by a variety of cell types other than platelets.
They act as potent mitogens for almost all mesenchymally-derived cells. Aberrant expression is involved in certain cancers, fibroproliferative disorders and atherosclerosis. The protein also contributes to wound healing and neural regeneration. There are four members of the PDGF family – PDGF A, PDGF B, PDGF C and PDGF D. Two distinct types of PDGF-A exist – a short form that is soluble and a long form that is retained by the extracellular matrix.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

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

Description:

Epidermal Growth Factor Receptor Human Recombinant Sf9, Active

Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

Product # :

PKA-335

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
biological activity
More Info

Description

EGFR Human Recombinant encoding a.a. 672-1210 expressed in Baculovirus infected Sf9 cells, fused with a GST-tag at N-terminus with thrombin cleavage sites, having a molecular weight of 89,171 Dalton.EGFR is purified by proprietary chromatographic techniques.

Source

Baculovirus infected Sf9 cells.

Formulation

EGFR in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT, 15mM reduced glutathione and 20% glycerol.

Biological Activity

Determination of Km value by Filter binding assay MAFC membrane.

More Info

Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
Synonyms
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
Physical Appearance
Sterile filtered liquid.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please avoid freeze-thaw cycles.
Specific Activity
30 pmol/µgxmin.

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:

Lipopolysaccharide-induced TNF factor, Mouse Anti Human

Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF, PIG7, SIMPLE, TP53I7, FLJ38636, MGC116698, MGC116700, MGC116701, MGC125274, MGC125275, MGC125276.

Product # :

ANT-443

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info

Formulation

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

More Info

Introduction
Lipopolysaccharide is a potent stimulator of monocytes and macrophages, causing secretion of tumor necrosis factor-alpha (TNF-alpha) and other inflammatory mediators. LITAF is a lipopolysaccharide-induced TNF-alpha factor, which is a DNA-binding protein and can mediate the TNF-alpha expression by direct binding to the promoter region of the TNF-alpha gene. The transcription of the LITAF gene is induced by tumor suppressor p53 and has been implicated in the p53-induced apoptotic pathway. Mutations in the LITAF gene cause Charcot-Marie-Tooth disease type 1C (CMT1C) and may be involved in the carcinogenesis of extramammary Paget''s disease (EMPD).
Synonyms
Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF, PIG7, SIMPLE, TP53I7, FLJ38636, MGC116698, MGC116700, MGC116701, MGC125274, MGC125275, MGC125276.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human LITAF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human LITAF amino acids 1-161 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT5C10AT.
Applications
LITAF antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1000. Recommended starting dilution is 1:1000.
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
LITAF antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

POU class 2 associating factor 1 Human Recombinant

POU domain class 2 associating factor 1, BOB-1, OCA-B, B-cell-specific coactivator OBF-1, OCT-binding factor 1.

Product # :

PRO-880

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

POU2AF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 276 amino acids (1-256) and having a molecular mass of 29.6 kDa.The POU2AF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

POU2AF1 protein (0.5mg/ml) is supplied in 20mM Tris-HCL, pH-8 and 20% Glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
POU2AF1 is a lymphocyte specific transcription coactivator protein. POU2AF1 cooperates only with the Oct1/2 proteins using sub domains in the POU domain of the Oct1/2 proteins, increasing their transcriptional efficiency. Even though POU2AF1 have no basic ability to bind DNA, it links firmly with the octomer motif in the presence of Oct1 and Oct2. POU2AF1 is expressed at maximum levels in spleen and peripheral blood leukocytes.
Synonyms
POU domain class 2 associating factor 1, BOB-1, OCA-B, B-cell-specific coactivator OBF-1, OCT-binding factor 1.
Physical Appearance
POU2AF1 is supplied as a 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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLWQKPTAPE QAPAPARPYQ GVRVKEPVKE LLRRKRGHAS SGAAPAPTAV VLPHQPLATY TTVGPSCLDM EGSVSAVTEE AALCAGWLSQ PTPATLQPLA PWTPYTEYVP HEAVSCPYSA DMYVQPVCPS YTVVGPSSVL TYASPPLITN VTTRSSATPA VGPPLEGPEH QAPLTYFPWP QPLSTLPTST LQYQPPAPAL PGPQFVQLPI SIPEPVLQDM EDPRRAASSL TIDKLLLEEE DSDAYALNHT LSVEGF

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-19 Human Recombinant, His Tag

Fibroblast growth factor 19, FGF-19.

Product # :

CYT-279

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

Fibroblast Growth Factor-19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 206 amino acids and having a molecular mass of 23 kDa. The amino acid sequence of the recombinant human FGF19 is 100% homologous to the amino acid sequence of the human FGF19 without signal sequence and contains his tag at N-terminal. The FGF-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% 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 19, FGF-19.
Physical Appearance
Filtered white lyophilized powder.
Stability
Lyophilized FGF-19 Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-19 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
Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MRGSHHHHHH GMASLAFSDA GPHVHYGWGD PIRLRHLYTS GPHGLSSCFL RIRADGVVDC ARGQSAHSLLEIKAVALRTV AIKGVHSVRY LCMGADGKMQ GLLQYSEEDC AFEEEIRPDG YNVYRSEKHR LPVSLSSAKQ RQLYKNRGFL PLSHFLPMLP MVPEEPEDLR GHLESDMFSS PLETDSMDPF GLVTGLEAVR SPSFEK.
Background
What is the molecular weight/Mw of FGF19 HUMAN,HIS Protein?
FGF19 HUMAN,HIS Protein has a total Mw of 23kDa.

What is the source or expression system of FGF19 HUMAN,HIS Protein?
Escherichia Coli.

What is the Purity of FGF19 HUMAN,HIS Protein?
FGF19 HUMAN,HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF19 HUMAN,HIS Protein?
The biological functionality of FGF19 HUMAN,HIS Protein will be determined in the future.

What is the amino acid sequence of FGF19 HUMAN,HIS Protein?
MRGSHHHHHH GMASLAFSDA GPHVHYGWGD PIRLRHLYTS GPHGLSSCFL RIRADGVVDC ARGQSAHSLLEIKAVALRTV AIKGVHSVRY LCMGADGKMQ GLLQYSEEDC AFEEEIRPDG YNVYRSEKHR LPVSLSSAKQ RQLYKNRGFL PLSHFLPMLP MVPEEPEDLR GHLESDMFSS PLETDSMDPF GLVTGLEAVR SPSFEK.

What applications can FGF19 HUMAN,HIS Protein be used in?
FGF19 HUMAN,HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF19 HUMAN,HIS Protein?
The endotoxin level is minimal, FGF19 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:

Transforming Growth Factor-Beta 3 Human Recombinant, Plant

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

Product # :

CYT-588

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

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

Source

Nicotiana benthamiana.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

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

More Info

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

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

Country/region

Search results

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Formulation

More Info

More Info

Description

Source

Formulation

Purity

SDS-PAGE

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

sds-page

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

sds-page

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info