Search: 774 results found for "transforming growth factor beta induced"

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.

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ANT-443

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Formulation

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

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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:

Brain-Derived Neurotrophic Factor Human Recombinant

Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

Product # :

CYT-207

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Activity

Description

BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

Purity

BDNF is greater than 950% as determined SDS-PAGE.

Biological Activity

The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

Activity

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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.

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

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

What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor 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:

Transcription Factor B2, Mitochondrial Human Recombinant

Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.

Product # :

PRO-1259

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Description

TFB2M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (20-396 a.a) and having a molecular mass of 45.8kDa.TFB2M is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TFB2M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Transcription Factor B2, Mitochondrial (TFB2M) is an S-adenosyl-L-methionine-dependent methyltransferase which specifically dimethylates mitochondrial 12S rRNA at the conserved stem loop. In addition, TFB2M is essential for basal transcription of mitochondrial DNA, most likely via its interaction with POLRMT and TFAM. TFB2M promotes transcription independently of the methyltransferase activity. TFB2M like TFB1M, activates transcription of mitochondrial DNA more effectively, whilst having less methyltransferase activity.
Synonyms
Dimethyladenosine transferase 2 mitochondrial, Hepatitis C virus NS5A-transactivated protein 5, HCV NS5A-transactivated protein 5, Mitochondrial 12S rRNA dimethylase 2, Mitochondrial transcription factor B2, h-mtTFB, h-mtTFB2, hTFB2M, mtTFB2, S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 2, TFB2M, NS5ATP5, Hkp1.
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 MGSMAGRFCI LGSEAATRKH LPARNHCGLS DSSPQLWPEP DFRNPPRKAS KASLDFKRYV TDRRLAETLA QIYLGKPSRP PHLLLECNPG PGILTQALLE AGAKVVALES DKTFIPHLES LGKNLDGKLR VIHCDFFKLD PRSGGVIKPP AMSSRGLFKN LGIEAVPWTA DIPLKVVGMF PSRGEKRALW KLAYDLYSCT SIYKFGRIEV NMFIGEKEFQ KLMADPGNPD LYHVLSVIWQ LACEIKVLHM EPWSSFDIYT RKGPLENPKR RELLDQLQQK LYLIQMIPRQ NLFTKNLTPM NYNIFFHLLK HCFGRRSATV IDHLRSLTPL DARDILMQIG KQEDEKVVNM HPQDFKTLFE TIERSKDCAY KWLYDETLED 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:

Tumor Necrosis Factor-Alpha Mutant Human Recombinant

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

Product # :

CYT-384

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Description

Tumor Necrosis Factor-a Variant Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 151 amino acids and having a molecular mass of 16598 Dalton. The TNF-alpha Variant is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized after extensive dialysis against 0.5x PBS pH -7.

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 cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 units/mg.

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Introduction
The clinical use of the potent anti-tumor activity of TNF-a has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-a mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-a, which binds to the murine TNF-R55 but not to the mouse TNF-R75, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-a, which binds to both murine TNF receptors. Based on these results, many TNF-? mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.
Recombinant Human TNF-a Variant/Mutant compared with the wild-type, has an amino acid sequence deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157 which is proven tohave more activity and with less inflammatory side effect in vivo.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a Variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a Variant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha Variant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN
QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIAF.

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

Description:

Epidermal Growth Factor Mouse Recombinant, Biotin

Urogastrone, URG, EGF.

Product # :

CYT-841

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered clear solution.
Stability
Should be stored at 4°C.Please do not freeze.
Amino Acid Sequence
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
Background
Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential
Abstract:
This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.
Introduction:
Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.
Protein Engineering and Biotin Conjugation:
EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.
Cellular Signaling Amplification:
The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.
Cellular Assays and Functional Responses:
In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.
Tailored Delivery Strategies:
The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.
Regenerative Medicine and Targeted Therapy:
The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.
Future Prospects and Challenges:
While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.
Conclusion:
In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.
What is the molecular weight/Mw of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein has a total Mw of 7kDa.

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

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

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

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

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

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

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

Description:

Epidermal Growth Factor Mouse Recombinant, His Tag

Urogastrone, URG, EGF.

Product # :

CYT-138

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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

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered 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:

Placental Growth Factor Human Recombinant

PIGF, PGF, PLGF-1

Product # :

CYT-1193

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Description

PLGF Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-170) containing 160 amino acids and having a molecular mass of 18.3kDa.PLGF is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

PLGF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Placental Growth Factor (PLGF) which is a member of the VEGF sub-family, is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. PLGFmainly plays a role in trophoblast growth and differentiation and binds to receptor vegfr-1/flt1.
Synonyms
PIGF, PGF, PLGF-1
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
DGSMAVPPQQ WALSAGNGSS EVEVVPFQEV WGRSYCRALE RLVDVVSEYP SEVEHMFSPS CVSLLRCTGC CGDENLHCVP VETANVTMQL LKIRSGDRPS YVELTFSQHV RCECRPLREK MKPERRRPKG RGKRRREKQR PTDCHLCGDA VPRRHHHHHH

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:

APRIL Human Recombinant

Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

Product # :

CYT-815

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sds-page

Description

APRIL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (105-247) and having a molecular mass of 17.6kDa.APRIL is fused to a 16 amino acid T7-tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APRIL 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

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Introduction
APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines.
Synonyms
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.
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
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.
Background
APRIL Human Recombinant: Expanding the Horizons of Immunotherapy
Abstract:

APRIL (A Proliferation-Inducing Ligand) is a promising molecule within the tumor necrosis factor (TNF) superfamily that plays a pivotal role in immune regulation. This research paper provides an overview of APRIL human recombinant, exploring its potential applications in immunotherapy. Understanding the mechanisms and therapeutic implications of APRIL holds promise in the field of immune-related disorders. This article presents a concise analysis of APRIL, highlighting its potential as a therapeutic target.
Introduction:

Immunotherapy has revolutionized the treatment of various diseases by harnessing the power of the immune system. APRIL, a member of the TNF superfamily, has emerged as a potential candidate for immunotherapeutic interventions. This paper provides an overview of APRIL, shedding light on its structure, function, and potential applications in immunotherapy.
APRIL Structure and Function:

APRIL is a transmembrane protein that can be proteolytically cleaved, leading to the generation of soluble forms. It interacts with its receptors, such as BCMA and TACI, to regulate immune responses. APRIL influences B-cell activation, proliferation, and antibody production, making it a compelling target for immunotherapeutic strategies.
Immunotherapeutic Applications of APRIL Human Recombinant:

APRIL human recombinant holds great potential in immunotherapy. By modulating APRIL activity, it may be possible to enhance immune responses against cancer cells or dampen immune dysregulation in autoimmune disorders. Additionally, APRIL-based therapeutics could be developed to target specific immune cell populations or enhance the efficacy of existing immunotherapies.
Challenges and Future Directions:

Although APRIL shows promise, there are challenges to overcome. Further research is needed to elucidate the precise mechanisms of APRIL-mediated immune regulation and identify optimal therapeutic approaches. Additionally, safety considerations and potential side effects must be thoroughly evaluated.
Conclusion:

APRIL human recombinant represents a valuable tool for advancing immunotherapy. Understanding the structure, function, and therapeutic potential of APRIL opens up new avenues for treating immune-related disorders. Continued research and development in this field have the potential to revolutionize the landscape of immunotherapy, improving patient outcomes and expanding the possibilities for personalized medicine.
What is the molecular weight/Mw of APRIL Protein?
APRIL Protein has a total Mw of 17.6kDa.

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

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

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

What is the amino acid sequence of APRIL Protein?
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

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

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

Macrophage Migration Inhibitory Factor Human Recombinant (Active)

Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.

Product # :

CYT-596

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Description

MIF human Recombinant was cloned into an E.coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chain containing 115 amino acids and having a molecular mass of 12.5 kDa.

Source

Escherichia Coli.

Formulation

MIF-Protein was lyophilized from 10mM sodium phosphate buffer pH-7.5.

Purity

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

Biological Activity

Human PBMCs were cultured with 0 to 1000ng/ml Human MIF. Production of IL-8 was measured via ELISA after 24 hours. The ED50 which was found to be 88-132ng/ml.

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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIF-protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF-protein 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 MIF-Protein in sterile 18MΩ-cm H2O at a concentration between 0.1mg-1mg per 1ml.
Amino Acid Sequence
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLM
AFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVY
INYYDMNAANVGWNNSTFA.

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

Description:

Growth and Differentiation factor 15 Mouse Recombinant

Growth/differentiation factor 15, GDF-15.

Product # :

CYT-857

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sds-page

Description

GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa. GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF15 protein solution (1.0mg/ml) containing 20mM Phosphate buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
GDF15 is part of the TGF-Beta superfamily which is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
Growth/differentiation factor 15, GDF-15.
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 MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.
Background
What is the molecular weight/Mw of GDF15 MOUSE Protein?
GDF15 MOUSE Protein has a total Mw of 14.9kDa.

What is the source or expression system of GDF15 MOUSE Protein?
Escherichia Coli.

What is the Purity of GDF15 MOUSE Protein?
GDF15 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 MOUSE Protein?
The biological functionality of GDF15 MOUSE Protein will be determined in the future.

What is the amino acid sequence of GDF15 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

What applications can GDF15 MOUSE Protein be used in?
GDF15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 MOUSE Protein?
The endotoxin level is minimal, GDF15 MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

Vascular Endothelial Growth Factor Rat Recombinant

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

Product # :

CYT-392

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Description

Vascular Endothelial Growth Factor Rat Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38,750 Dalton. The VEGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 10mM NaP, pH 7.5.

Purity

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

Biological Activity

Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 4.0-8.0 ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vascular Endothelial Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTTEGEQK AHEVVKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNVTMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC 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:

Fibroblast Growth Factor Receptor 4 Fc Chimera Human Recombinant

Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.

Product # :

PKA-233

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Description

Soluble FGFR-4a (IIIc) Fc Chimera Human Recombinant fused with Xa cleavage site with the Fc part of human IgG1 produced in baculovirus is a heterodimeric, glycosylated, Polypeptide chain and having a molecular mass of 170 kDa. The FGFR4 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

CD334 was lyophilized from a concentrated (1mg/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

Determined by its ability to inhibit human FGF acidic-dependent proliferation on R1 cells. The ED50 for this effect is typically at 15.0-30.0 ng/ml.

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Introduction
Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.
Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGFR4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFR4 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 FGFR-4 in sterile PBS not less than 100 µg/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:

Interleukin-1 beta Rat Recombinant

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

Product # :

CYT-394

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Description

Interleukin-1b Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17.3 kDa.The IL-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 0.2um filtered concentrated solution in PBS, pH 7.4, 5% trehalose and 0.02 % Tween-20.

Purity

Greater than 96.0% as determined by:

(a) Analysis by RP-HPLC.

(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ was found to be less than 0.1ng/ml, determined by the dose dependent proliferation of mouse D10S cells, corresponding to a specific activity of 10,000,000 units/mg.

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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b 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 Interleukin 1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MVPIRQLHCRLRDEQQKCLVLSDPCELKALHLNGQNISQQVVFSMSF
VQGETSNDKIPVALGLKGLNLYLSCVMKDGTPTLQLESVDPKQYPKK
KMEKRFVFNKIEVKTKVEFESAQFPNWYISTSQAEHRPVFLGNSNGRD
IVDFTMEPVSS.

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/APO 2 Ligand (114-281 a.a.) 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-546

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Description

Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml in 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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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 colorless liquid.
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
MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.

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:

Melanoma Inhibitory Activity Protein Human Recombinant, His Tag

Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.

Product # :

CYT-810

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Description

MIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (25-131) and having a molecular mass of 14.4 kDa.MIA is fused to a 21 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.
Synonyms
Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.
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 MGPMPKLADR KLCADQECSH PISMAVALQD YMAPDCRFLT IHRGQVVYVF SKLKGRGRLF WGGSVQGDYY GDLAARLGYF PSSIVREDQT LKPGKVDVKT DKWDFYCQ

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:

Stem Cell Factor Human Recombinant, HEK

Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.

Product # :

CYT-111

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Quantity :

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Description

SCF Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 35-45kDa due to glycosylation.The SCF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

SCF was lyophilized from a 0.2µm filtered solution (1mg/ml) containing 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line).
The EC₅₀ is 15.25ng/ml.

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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 SCF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

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

Description:

TRAIL Receptor-1 Human Recombinant Fc

Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.

Product # :

CYT-877

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Description

TRAIL R1 Fc Human Recombinant (24-240) produced in E.Coli is a non-glycosylated, disulfide-linked homodimer containing two polypeptide chains of 217 amino acids each and having a molecular mass of 41kDa [including tag] each chain. TRAILR1 is fused to a 236 amino acid Fc tag at C-terminal and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by its ability to inhibit Trail-mediated cytotoxicity in mouse L-929 cells, is less than 1.25ng/ml.

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Introduction
Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFRSF10A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL-R1 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 TNFRSF10A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSERPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSTGCPR GMVKVKDCTP WSDIECVHKE SGNGHNIEGR MDPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK.

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

Description:

Macrophage Colony Stimulating Factor Human Recombinant, His Tag

CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

Product # :

CYT-695

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Quantity :

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Description

Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 179 amino acids (33-190 a.a.) and having a total molecular mass of 20.7 kDa.MCSF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MCSF protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT & 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
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 MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ DVVTKPDCN.

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:

Hypoxia-Inducible Factor-1 Alpha Human Recombinant, His Tag

Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

Product # :

PRO-415

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Description

HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (576-785 a.a.) and having a molecular mass of 25.1 kDa. The HIF1A is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HIF1A Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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 MSFDQLSPLE SSSASPESAS PQSTVTVFQQ TQIQEPTANA TTTTATTDEL KTVTKDRMED IKILIASPSP THIHKETTSA TSSPYRDTQS RTASPNRAGK GVIEQTEKSH PRSPNVLSVA LSQRTTVPEE ELNPKILALQ NAQRKRKMEH DGSLFQAVGI GTLLQQPDDH AATTSLSWKR VKGCKSSEQN GMEQKTIILI PSDLACRLLG Q.

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

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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.

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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:

Signal Sequence Receptor, Beta Human Recombinant

HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.

Product # :

PRO-1380

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Description

SSR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (18-149a.a) and having a molecular mass of 16.8kDa. SSR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

SSR2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum membrane receptor related with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The human beta-signal sequence receptor gene (SSR2) maps to chromosome bands 1q21-q23. Diseases correlated with SSR2 include calcaneonavicular coalition, and osteosarcoma, and among its related super-pathways are Viral mRNA Translation and Generic Transcription Pathway.
Synonyms
HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.
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 MGSEEGARLL ASKSLLNRYA VEGRDLTLQY NIYNVGSSAA LDVELSDDSF PPEDFGIVSG MLNVKWDRIA PASNVSHTVV LRPLKAGYFN FTSATITYLA QEDGPVVIGS TSAPGQGGIL AQREFDRRFS PHFLD.

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

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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.

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Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and 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:

IGF-1 Human Recombinant

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

Product # :

CYT-216

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Introduction
The somatomedins, IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B.
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IGF-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Background
IGF stands for INS like growth factors, which are proteins that have a high similarity to INS. They are part of a complicated process that uses cells to communication with the physiologic environment around them. IGF’s complex system is often called the ‘axis’. This consists of:
● Two cell-surface receptors (IGF1R and IGF2R)
● Two ligands (IGF-1 and IGF-2)
● A family of six high-affinity IGF-binding proteins.
● Proteases.
The Effect IGF Has On The Body
Many unique tissue types express the IGF-1 receptor, and the effects can vary. It induces the survival of neurons, may catalyse skeletal muscle hypertrophy by inducing protein synthesis, and by blocking muscle atrophy. It works as a protector for cartilage cells, and may work to be an anabolic factor for the bones. When used in high concentrations, it can activate the INS receptor, and can even complement the effects that INS has on the body.
Diseases And IGF
Diseases and IGF are closely related, and a number of them can be affected. The INS IGF axis is thought to have an effect on aging, with an increased life span shown in fruit flies when used in studies.
It is also important to note the crucial role that IGF plays in cancer and diabetes - IGF- 1 has been shown to stimulate growth in both prostate and breast cancer cells. The degree of risk that IGF-1 poses is up for debate, and many scientists are not in agreement. IGF has also shown to have the ability to decrease blood glucose levels, although not quite as effective as INS.
How Was IGF Discovered?
Investigators began studying the effects of biological substances on cells and tissues outside the body when IGFs were discovered. The name is self explanatory in the fact that IGF performs INS actions in some tissues, but is less potent than INS at decreasing blood sugar. Its fundamental action is to stimulate growth, whether that be within the epidermal growth factor or the nerve growth factor.
What’s The Difference Between IGF-1 And IGF-2?
The two types of IGF are IGF-1 and IGF-2. Although the names are similar, the specific actions that they take are different - they bind and activate completely difference receptors. The major actor in them both is the effect that they have on cell growth. Most of the actions of the pituitary GH are mediated by IGFs, but predominantly IGF-1. GH works to stimulate many tissues within the body, especially the liver which then secretes IGF-1. This then causes hypertrophy, or in layman's terms, an increase in cell size, as well as hyperplasia which is an increase in the number of cells.
The IGF-1 concentration will increase during childhood and hit peak during puberty, but will then decrease afterwards, as does the hormone secretion itself. It has been proven that children and adults with a deficiency of the GH have low serum IGF-1 concentrations when put in comparison with others in the same age range. Patients who have conditions like acromegaly have been shown to have increased serum IGF-1 concentrations. The production of IGF-2 is less dependent on the secretion of GH than IGF-1, and is much less important for stimulating linear growth.
What is the molecular weight/Mw of IGF1 HUMAN Protein?
IGF1 HUMAN Protein has a total Mw of 7.6kDa.

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

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

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

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

What is the endotoxin level for IGF1 HUMAN Protein?
The endotoxin level is minimal, IGF1 HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Eukaryotic Translation Elongation Factor 1 Beta 2 Human Recombinant

Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.

Product # :

PRO-167

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Description

EEF1B2 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 233 amino acids (1-225 a.a.) and having a molecular mass of 25.8kDa. The EEF1B2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EEF1B2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 100mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Elongation factor 1-beta (EEF1B2) is a translation elongation factor. EEF1B2 is a guanine nucleotide exchange factor which is involved in the transfer of aminoacylated tRNAs to the ribosome. Both EEF1B2 and EEF1D stimulate the exchange of GDP bound to EEF1A to GTP.
Synonyms
Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.
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
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKILEHHH 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.

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