Search: 1000 results found for "neurotrophic factors"

Description:

Epidermal Growth Factor (Leu-21) Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-466

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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

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

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

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

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

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

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

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

Description:

Hepatocyte Growth Factor Human Recombinant, CHO

Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

Product # :

CYT-251

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Hepatocyte Growth Factor Human Recombinant produced in CHO is a heterodimer, non-glycosylated, polypeptide chain consisting an a-chain of 463 amino acids and b-chain of 234 having a total molecular mass of approximately 75kDa. The HGF is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovarian Cells.

Formulation

The protein was lyophilized from a concentrated (1.4mg/ml) solution containing Phosphate-Buffered Saline with 0.02% Tween 80, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

More Info

Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Hepatocyte Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte 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
Agrees with the sequence of native human HGF.
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein has a total Mw of 75kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
Chinese Hamster Ovarian Cells.

What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
Agrees with the sequence of native human HGF.

What applications can HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein be used in?
HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN, CHO 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

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

Product # :

CYT-368

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

TGF-β 3 Human Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.8kDa. The TGF-β 3 is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein solution contains 20% Ethanol and 10mM Acetic acid (AcOH).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

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

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 clear solution.
Stability
TGF-beta 3 although stable at room temperature for 1 week, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Amino Acid Sequence
MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Background
TGFB3 (207 a.a.) Human

About TGFB3 (207 a.a.) Human:
Transforming growth factor beta-3 (also known as TGF-β3) is a cytokine encoded by the TGFB3 gene that belongs to the transforming growth factor beta superfamily. It plays a significant role in cell differentiation, embryogenesis, and development by regulating molecules involved in cell adhesion and extracellular matrix formation. TGF-β3 is necessary for palate development, as its absence causes clefting. In addition, it controls lung development and wound healing processes by regulating cell adhesion and movement in the respective tissues. Together, TGF-β3 coordinates a variety of cellular processes that are critical for mammalian embryonic development and tissue homeostasis. In this article we will explore the features and applications of TGFB3 Human Recombinant Protein, expanding on its significance in in advanced research pursuits.
Description:
TGFB3 Human Recombinant protein encodes amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag). As TGFB3 Human derives from Escherichia Coli, it appears as a sterile filtered clear solution and is formulated as 100µl of purified human TGF Beta 3 protein at 100µg/ml. In addition, its protein is formulated in a solution comprising 50mM Tris-Acetate (pH 7.5), 1mM EDTA, and 20% Glycerol. In terms of stability, TGF-beta 3 Human Recombinant is stable at 4°C for up to a week. However, it is preferable to store at -20°C. However, if you are looking to store it for a long term it is preferable to add a carrier protein (0.1% HSA or BSA).
Activation:
While TGF-β plays a crucial role regulating essential cell functions, its activation pathways is still being explored and understood. Some pathways are specific to certain cells or tissues, while others are more widespread. Factors like proteases, integrins, pH, and reactive oxygen species can activate TGF-β. Disruptions in these factors can lead to uncontrolled TGF-β signaling, causing issues like inflammation, autoimmune diseases, and cancer.
Applications and Usage:
TGFB3 (207 a.a.) Human is intended for laboratory research, serving as an important tool in stem cell differentiation as well as T-cell regulation and differentiation. Accordingly, its versatility extends to applications such as ELISA, Western Blotting, and Inhibition Assays, offering different avenues for discovery and research.
Safety Information:
TGFB3 (207 a.a.) Human is intended for use only in laboratory research, in accordance with safety guidelines. It emphasizes adherence to ethical and regulatory norms and is not intended for use as household chemicals, pharmaceuticals, agricultural products, or food additives.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 as a Reference Standard.

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

Description:

GM-CSF Receptor Alpha Human Recombinant

CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

Product # :

CYT-796

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page

Description

CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CSF2RA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
Synonyms
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.
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.
Background
Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.
Therapeutic Applications:
Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.
Challenges and Future Directions:
While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 37.2kDa.

What is the source or expression system of CD116 Protein?
Escherichia Coli.

What is the Purity of CD116 Protein?
CD116 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CD116 Protein?
The biological functionality of CD116 Protein will be determined in the future.

What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 324 amino acids.

What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 Protein was purified using conventional chromatography techniques.

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

Description:

Vascular Endothelial Growth Factor receptor-1 Human Recombinant, His Tag

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-354

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

FLT1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 298 amino acids fragment (31-328) corresponding to the IgG like domains 1-3 from the mature soluble FLT1 protein, having a total molecular mass of 43kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The FLT1 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FLT1 His-Tag protein is supplied in 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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:

Fibroblast Growth Factor-acidic (154 a.a.) Human Recombinant

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Product # :

CYT-1112

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 17.3kDa. The FGF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4, with 0.5mM DTT, 2mM EDTA, and 5 % Trehalose.

Purity

Greater than 97.0% as determined by:

(a) Analysis by RP-HPLC.

(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×10⁶IU/mg in the presence of 10µg/ml Heparin.

More Info

Introduction
Acidic fibroblast growth factor 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. FGF1 functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor.FGF1 acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-acidic 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 Fibroblast Growth Factor-acidic Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF 1 Protein?
Escherichia Coli.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×106 IU/mg in the presence of 10µg/ml Heparin.

What is the amino acid sequence of FGF 1 Protein?
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 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 2 Rat Recombinant

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

Product # :

CYT-1267

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Transforming Growth Factor-Beta 2 Rat Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 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 TGFB2 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.

More Info

Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.
Background
Rat TGFB22 signals through TGFBR2, TGFBR1 using an accessory co-receptor TGFBR3 (betaglycan) that enhances presentation of TGFβ2
Rat TGFB2 is a potent inducer of epithelial–mesenchymal transition (EMT) therefore is used in Cancer metastasis, Fibrosis, Retinal disorders, Developmental biology and Wound healing

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

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

What is the molecular weight / Mw of Rat TGFB2 Protein?
Rat TGFB2 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Rat TGFB2 Protein?
The biological functionality of Rat TGFB2 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Rat TGFB2 Protein?
The endotoxin level is minimal, Rat TGFB2 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Rat TGF beta 2 Protein?
If there is sequence put it instead of the sentence

Is TGFB2 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:

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:

Nephroblastoma Overexpressed Human Recombinant

Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

Product # :

CYT-805

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.

Purity

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

Biological Activity

Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

More Info

Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV 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 NOV in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.

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

Fibroblast growth factor 19, FGF-19, FGF19.

Product # :

CYT-700

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

FGF19 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.8 kDa.The FGF-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from 1mg/ml in 1xPBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of balb/c 3T3 cells is 100-150ng/ml.

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 INS desensitization and to improve INS, 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, FGF19.
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
It is recommended to reconstitute the lyophilized FGF-19 in sterile 1X PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRPLAFSDAG PHVHYGWGDP IRLRHLYTSG PHGLSSCFLR IRADGVVDCA RGQSAHSLLE IKAVALRTVA IKGVHSVRYL CMGADGKMQG LLQYSEEDCA FEEEIRPDGY NVYRSEKHRL PVSLSSAKQR QLYKNRGFLP LSHFLPMLPM VPEEPEDLRG HLESDMFSSP LETDSMDPFG LVTGLEAVRS PSFEK.
Background
What is the molecular weight/Mw of FGF19 Protein?
FGF19 Protein has a total Mw of 21.8kDa.

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

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

What is the Biological Activity of FGF19 Protein?
The ED50 as determined by the dose-dependent stimulation of the proliferation of balb/c 3T3 cells is 100-150ng/ml.

What is the amino acid sequence of FGF19 Protein?
MRPLAFSDAG PHVHYGWGDP IRLRHLYTSG PHGLSSCFLR IRADGVVDCA RGQSAHSLLE IKAVALRTVA IKGVHSVRYL CMGADGKMQG LLQYSEEDCA FEEEIRPDGY NVYRSEKHRL PVSLSSAKQR QLYKNRGFLP LSHFLPMLPM VPEEPEDLRG HLESDMFSSP LETDSMDPFG LVTGLEAVRS PSFEK.

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

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

Neuropoietin Mouse Recombinant

Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.

Product # :

CYT-1128

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.

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 human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

More Info

Introduction
CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.
Synonyms
Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin 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 Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.
Background
What is the molecular weight/Mw of CTF2P Protein?
CTF2P Protein has a total Mw of 19.7kDa.

What is the source or expression system of CTF2P Protein?
Escherichia Coli.

What is the Purity of CTF2P Protein?
CTF2P Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF2P Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.

What is the amino acid sequence of CTF2P Protein?
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.

What applications can CTF2P Protein be used in?
CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF2P Protein?
The endotoxin level is minimal, CTF2P Protein was purified using conventional chromatography techniques.

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

Description:

Keratinocye Growth Factor Mouse Recombinant

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

Product # :

CYT-721

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

More Info

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

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

Description:

Vascular Endothelial Growth Factor C Human Recombinant, Sf9

Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein.

Product # :

CYT-948

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

VEGFC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 125 amino acids (112-227a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). VEGFC is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

VEGFC protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.
Synonyms
Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein.
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
ADPAHYNTEI LKSIDNEWRK TQCMPREVCI DVGKEFGVAT NTFFKPPCVS VYRCGGCCNS EGLQCMNTST SYLSKTLFEI TVPLSQGPKP VTISFANHTS CRCMSKLDVY RQVHSIIRRH HHHHH.

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

Description:

Transforming Growth Factor-Beta 3 Human Recombinant, HEK

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

Product # :

CYT-113

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

TGF-beta 3 Human Recombinant produced in HEK cells is a homodimer containing 2 x 112 amino acids linked by a disulfide bond having a total molecular weight of 25kDa. The TGF-b 3 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The TGF-b 3 was lyophilized from 1mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent inhibition of IL-4 induced proliferation of mouse HT-2 cells (BALB/c spleen activated by sheep erythrocytes in the presence of IL-2) and is typically 0.05 ng/ml corresponding to a specific activity of ≥ 20,000,000 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 TGF-b 3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-b 3 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 TGF-b 3 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.
Amino Acid Sequence
MALDTNYCFR NLEENCCVRP LYIDFRQDLG WKWVHEPKGY YANFCSGPCP YLRSADTTHS TVLGLYNTLN PEASASPCCV PQDLEPLTIL YYVGRTPKVE QLSNMVVKSC KCS

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 Human Recombinant, Yeast

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

Product # :

CYT-577

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

Vascular Endothelial Growth Factor Human Recombinant produced in Yeast is a double, glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 42 kDa.

Source

Pichia Pastoris.

Formulation

The protein contains 20mM Phosphate- Buffered Saline, pH 7.4.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Determined by its ability to stimulate 3H-Thymidine incorporation in human umbilical vein endothelial cells, the ED50 for this effect was found to be 2-6ng/ml.

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/macrophage migration, 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 mitogenesis and 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.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered colorless liquid formulation.
Stability
Vascular Endothelial Growth Factor Human although stable at 15°C for 2 weeks, should be stored 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.

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 Mouse Recombinant, Sf9

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

Product # :

CYT-226

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Vascular Endothelial Growth Factor Mouse Recombinant produced in Sf9 insect cells is a double, glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 48 kDa.The VEGF is purified by proprietary chromatographic techniques.

Source

Baculovirus Sf9 cells.

Formulation

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

Purity

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

Biological Activity

The ED₅₀ range, determined by the dose-dependent proliferation of human umbilical vein endothelial cells (HUVEC) (measured by ³H-thymidine uptake) is 1-2 ng/ml, corresponding to a specific activity of 1x10⁶ Units/mg.

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
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vascular Endothelial Growth Factor Sf9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-Sf9 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 Vascular Endothelial Growth Factor-Sf9 in sterile 18MΩ-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:

Nephroblastoma Overexpressed Human Recombinant, HEK

Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

Product # :

CYT-1032

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).

Source

HEK293 cells.

Formulation

NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NOV is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH 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:

TNF Ligand Receptor Superfamily Member 12A Human Recombinant

Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

Product # :

CYT-043

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

TNFRSF12A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 5.6 KDa.The TNFRSF12A 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 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The TNFRSF12A biological activity is determined by its ability to inhibit TWEAK-induced weak cell death of HT29 cells. The expected ED50 for this effect is 1.0-5.0ug/ml in the presence of 1ug/ml rhTWEAK.

More Info

Introduction
The gene for TNFRSF12A was initially recognized as a fibroblast growth factor inducible immediate early response gene Fn14 in mouse NIH 3T3 fibroblasts. Human TNFRSF12A cDNA encodes a 129 amino acid residue type I transmembrane protein with a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. Human and mouse TNFRSF12A hold 82% aa sequence identity. TNFRSF12 is the tiniest member of the TNF receptor superfamily and has only one cysteine rich region in its extracellular domain. The TNFRSF12A cytoplasmic domain holds one TRAF binding motif which binds TRAFs 1, 2, and 3. TNFRSF12A binds its ligand TWEAK/TNFSF12A with high affinity to initiate a signal transduction cascade which subject to the cell type, causes different cellular responses such as cell death, cell proliferation, and angiogenesis.
Synonyms
Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFRSF12A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFRSF12A 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 TNFRSF12A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWP.

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 1 Human Recombinant, His Tag

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.

Product # :

CYT-672

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (279-390) having a molecular weight of 17.3kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TGF-b 1 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TGF-b 1 His-Tag protein is supplied in 25mM NaAcetate pH 4.8 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 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.
TGF-b 1 regulates the actions of numerous other growth factors involved in a variety of human diseases including renal disease, hepatic disease, heart failure and cardiomyopathies.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.
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:

RANK Ligand Soluble Mouse Recombinant

Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.

Product # :

CYT-320

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

sRANKL Mouse Recombinant produced in E.coli is single, non-glycosylated, polypeptide chain containing 174 amino acids ( 143-316 a.a.) and having a total molecular mass of 19.9kDa. CD254 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized with 10mM Na2PO4, pH 7.5 & 50mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to induce osteoclast formation on murine RAW264.7 cells using a concentration of 50ng/ml shown in “Corning® Osteo Assay Surface 24 Well Plates with Transwell® Permeable Supports- A Useful Tool for Co-Culture Studies” by Rebecca M. Wood and Mark Rothenber, corresponding to a specific activity of 20,000Units/mg.

More Info

Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL 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 sRANKL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
PAMMEGSWLD VAQRGKPEAQ PFAHLTINAA SIPSGSHKVT LSSWYHDRGW AKISNMTLSN GKLRVNQDGF YYLYANICFR HHETSGSVPT DYLQLMVYVV KTSIKIPSSH NLMKGGSTKN WSGNSEFHFY SINVGGFFKL RAGEEISIQV SNPSLLDPDQ DATYFGAFKV QDID.

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:

Myostatin Propeptide Human Recombinant, HEK

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

CYT-936

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

Myostatin Propetide Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Arg266) containing a total of 253 amino acids, having a calculated molecular mass of 29.1kDa. Myostatin Propetide is fused to a 10 aa C-terminal His tag.

Source

HEK 293.

Formulation

Myostatin Propetide solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Physical Appearance
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
NENSEQKENV EKEGLCNACT WRQNTKSSRI EAIKIQILSK LRLETAPNIS KDVIRQLLPK APPLRELIDQ YDVQRDDSSD GSLEDDDYHA TTETIITMPT ESDFLMQVDG KPKCCFFKFS SKIQYNKVVK AQLWIYLRPV ETPTTVFVQI LRLIKPMKDG TRYTGIRSLK LDMNPGTGIW QSIDVKTVLQ NWLKQPESNL GIEIKALDEN GHDLAVTFPG PGEDGLNPFL EVKVTDTPKR SRR HHHHHHH HHH.

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 2 Human Recombinant, CHO

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

Product # :

CYT-1268

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

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

Source

CHO Cells.

Formulation

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

Purity

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

Biological Activity

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

More Info

Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS.
Background
Recombinant TGFB2 protein is used in cell culture to study extracellular matrix remodelling, tissue regeneration, and developmental biology.
TGFB2 takes part in embryonic development and is involved in fibrosis, wound healing, angiogenesis,

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

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

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

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

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

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

What is the endotoxin level for TGFB2 Protein?
The endotoxin level is minimal, TGFB2 Protein was purified using conventional chromatography techniques.

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

Description:

Fibroblast Growth Factor-18 Human Recombinant, His Tag

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

Product # :

CYT-935

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

FGF18 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu28-Ala207) containing 190 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22.3kDa.

Source

Escherichia Coli.

Formulation

FGF18 was filtered (0.4µm) and lyophilized in phosphate buffered saline and 5% w/v trehalose.

Purity

Purity as determined by densitometric image analysis is greater than 95%.

More Info

Introduction
Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.
Synonyms
Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FGF18 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.
Background
What is the molecular weight/Mw of FGF18 HIS Protein?
FGF18 HIS Protein has a total Mw of 22.3kDa.

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

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

What is the Biological Activity of FGF18 HIS Protein?
The biological functionality of FGF18 HIS Protein will be determined in the future.

What is the amino acid sequence of FGF18 HIS Protein?
MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.

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

What is the endotoxin level for FGF18 HIS Protein?
The endotoxin level is minimal, FGF18 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:

Vascular Endothelial Growth Factor Receptor-1 D5 Human Recombinant

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-239

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Soluble FLT1 D1-5 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 562 amino acids and having a molecular mass of 70 kDa. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT1 D1-5 was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.

Purity

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

Biological Activity

The activity of FLT1 D5 was determined by its ability to abolish the binding of iodinated VEGF to solid surfaces or cell surfaces. The ED50 for this effect is typically 10 ng/ml, corresponding to a specific activity of 100,000IU/mg.
In a 13 day CAM-assay sVEGFR-1 is able to inhibit VEGF stimulated sprouting of capillaries at 30 pM.

More Info

Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 D5 in sterile water 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.

Country/region

Search results

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

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

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