Search: 1000 results found for "insulin-like growth factor"

Description:

Angiopoietin-like Protein 4 Human Recombinant, HEK

ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.

Product # :

CYT-698

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Shipped at Room temp

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Description

The ANGPTL4 Human Recombinant is manufactured with C-terminal fusion of 11 amino acid FLAG Tag. The ANGPTL4 Flag -Tagged Fusion Protein is a 44.2kDa protein containing 392 amino acid residues of the Angiopoietin-like Protein 4 and 11 additional amino acid residues - Flag Tag (underlined).

Source

HEK293.

Formulation

Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
The fasting-induced adipose factor (FIAF, ANGPTL4, PGAR, HFARP) was identified as an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. At the protein level, in human and mouse blood plasma, FIAF was found to be present both as a native protein and in a truncated form. Differentiation of mouse 3T3-L1 adipocytes was associated with the production of truncated FIAF, whereas in human white adipose tissue and SGBS adipocytes, only the native FIAF could be detected. Interestingly, the truncated FIAF was produced by human liver.
Experimental data suggest that FIAF is mainly presented in human blood plasma in a truncated form (FIAF-S2), whose level is increased by fenofibrate treatment. Levels of both truncated and native FIAF showed marked inter individual variation but were not associated with body mass index and were not influenced by prolonged semistarvation.
Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Angiopoietin-like Protein 4 Human recombinant 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
Add pyrogen free water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
GPVQSKSPRF ASWDEMNVLA HGLLQLGQGL REHAERTRSQ LSALERRLSA CGSACQGTEG STDLPLAPES RVDPEVLHSL QTQLKAQNSR IQQLFHKVAQ QQRHLEKQHL RIQHLQSQFG LLDHKHLDHE VAKPARRKRL PEMAQPVDPA HNVSRLHRLP RDCQELFQVG ERQSGLFEIQ PQGSPPFLVN CKMTSDGGWT VIQRRHDGSV DFNRPWEAYK AGFGDPHGEF WLGLEKVHSI TGDRNSRLAV QLRDWDGNAE LLQFSVHLGG EDTAYSLQLT APVAGQLGAT TVPPSGLSVP FSTWDQDHDL RRDKNCAKSL SGGWWFGTCS HSNLNGQYFR SIPQQRQKLK KGIFWKTWRG RYYPLQATTM LIQPMAAEAA SAAADYKDDDDK.
Applications
Western blotting.
Background
What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 44.2kDa.

What is the source or expression system of ANGPTL4 Protein?
HEK293.

What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL4 Protein?
GPVQSKSPRF ASWDEMNVLA HGLLQLGQGL REHAERTRSQ LSALERRLSA CGSACQGTEG STDLPLAPES RVDPEVLHSL QTQLKAQNSR IQQLFHKVAQ QQRHLEKQHL RIQHLQSQFG LLDHKHLDHE VAKPARRKRL PEMAQPVDPA HNVSRLHRLP RDCQELFQVG ERQSGLFEIQ PQGSPPFLVN CKMTSDGGWT VIQRRHDGSV DFNRPWEAYK AGFGDPHGEF WLGLEKVHSI TGDRNSRLAV QLRDWDGNAE LLQFSVHLGG EDTAYSLQLT APVAGQLGAT TVPPSGLSVP FSTWDQDHDL RRDKNCAKSL SGGWWFGTCS HSNLNGQYFR SIPQQRQKLK KGIFWKTWRG RYYPLQATTM LIQPMAAEAA SAAADYKDDDDK.

What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 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:

JAZF zinc finger 1 Human Recombinant

Juxtaposed with another zinc finger protein 1 , TAK1-interacting protein 27, Zinc finger protein 802, JAZF1, TIP27, ZNF802, JAZF zinc finger 1, Juxtaposed With Another Zinc Finger Gene 1.

Product # :

PRO-1444

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Description

JAZF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243 a.a) and having a molecular mass of 29.5kDa.JAZF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

JAZF1 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.

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Introduction
JAZF zinc finger 1 (JAZF1) is a nuclear protein with 3 C2H2-type zinc fingers, which functions as a transcriptional repressor. Chromosomal anomalies involving the JAZF1 are linked with endometrial stromal tumors. Alternatively spliced variants which encode different protein isoforms have been described; though, not all variants have been fully characterized.
Synonyms
Juxtaposed with another zinc finger protein 1 , TAK1-interacting protein 27, Zinc finger protein 802, JAZF1, TIP27, ZNF802, JAZF zinc finger 1, Juxtaposed With Another Zinc Finger Gene 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTGIAAA SFFSNTCRFG GCGLHFPTLA DLIEHIEDNH IDTDPRVLEK QELQQPTYVA LSYINRFMTD AARREQESLK KKIQPKLSLT LSSSVSRGNV STPPRHSSGS LTPPVTPPIT PSSSFRSSTP TGSEYDEEEV DYEESDSDES WTTESAISSE AILSSMCMNG GEEKPFACPV PGCKKRYKNV NGIKYHAKNG HRTQIRVRKP FKCRCGKSYK TAQGLRHHTI NFHPPVSAEI IRKMQQ

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:

Sulfatase Modifying Factor 1 Human Recombinant, Sf9

SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 1.

Product # :

PRO-2619

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Description

SUMF1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 347 amino acids (34-374.a.) and having a molecular mass of 38.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). SUMF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

SUMF1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
SUMF1 is a part of the SUMF protein family. SUMF1 catalyzes the hydrolysis of sulfate esters by oxidizing a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue called C-alpha-formylglycine. Mutations in this gene will cause multiple sulfatase deficiency meaning a lysosomal storage disorder.
Synonyms
SUMF1, AAPA3037, FGE, UNQ3037, Formylglycine-generating enzyme, C-alpha-formylglycine-generating enzyme 1, Sulfatase-modifying factor 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
SQEAGTGAGA GSLAGSCGCG TPQRPGAHGS SAAAHRYSRE ANAPGPVPGE RQLAHSKMVP IPAGVFTMGT DDPQIKQDGE APARRVTIDA FYMDAYEVSN TEFEKFVNST GYLTEAEKFG DSFVFEGMLS EQVKTNIQQA VAAAPWWLPV KGANWRHPEG PDSTILHRPD HPVLHVSWND AVAYCTWAGK RLPTEAEWEY SCRGGLHNRL FPWGNKLQPK GQHYANIWQG EFPVTNTGED GFQGTAPVDA FPPNGYGLYN IVGNAWEWTS DWWTVHHSVE ETLNPKGPPS GKDRVKKGGS YMCHRSYCYR YRCAARSQNT PDSSASNLGF RCAADRLPTM DHHHHHH.

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-3, Mouse Anti-Human

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

ANT-106

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IL-3.
Ig Subclass
Mouse Ig.
Clone
hIL3-E2.
Applications
Direct ELISA, Western Blot, Immuneprecipitation, Immunohistochemistry.
Titer
By direct ELISA, 1:1,000 dilution will yield 0.2 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion Exchange.

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:

ASF1 Anti-Silencing Function 1 Homolog B Human Recombinant

Histone chaperone ASF1B, Anti-silencing function protein 1 homolog B, hAsf1, hAsf1b, CCG1-interacting factor A-II, CIA-II, hCIA-II, ASF1B.

Product # :

PRO-1163

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Description

ASF1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-202 a.a) and having a molecular mass of 23.4kDa.ASF1B is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ASF1B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
ASF1 Anti-Silencing Function 1 Homolog B (ASF1B) belongs to the H3/H4 family of histone chaperone proteins and is similar to the anti-silencing function-1 protein in yeast. ASF1B is the substrate of the tousled-like kinase family of cell cycle-regulated kinases, and may have a crucial role in modulating the nucleosome structure of chromatin by guaranteeing a regular supply of histones at sites of nucleosome assembly. ASF1B cooperates with CAF-1 (chromatin assembly factor 1) to stimulate replication-dependent chromatin assembly. ASF1B is highly expressed in the testis and at lower levels in colon, small intestine and thymus. ASF1B is necessary for spermatogenesis.
Synonyms
Histone chaperone ASF1B, Anti-silencing function protein 1 homolog B, hAsf1, hAsf1b, CCG1-interacting factor A-II, CIA-II, hCIA-II, ASF1B.
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
MAKVSVLNVA VLENPSPFHS PFRFEISFEC SEALADDLEW KIIYVGSAES EEFDQILDSV LVGPVPAGRH MFVFQADAPN PSLIPETDAV GVTVVLITCT YHGQEFIRVG YYVNNEYLNP ELRENPPMKP DFSQLQRNIL ASNPRVTRFH INWDNNMDRL EAIETQDPSL GCGLPLNCTP
IKGLGLPGCI PGLLPENSMD CILEHHHHHH.

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

Description:

Bone Morphogenetic protein Receptor-1B Human Recombinant

Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.

Product # :

CYT-897

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Description

BMPR1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (14-126 a.a) and having a molecular mass of 15.1kDa. BMPR1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMPR1B protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Bone Morphogenetic protein Receptor-1B, also known as BMPR1B belongs to the TKL Ser/Thr protein kinase family. BMPR1Bis on ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate as well as activate type I receptors which autophosphorylate, afterward bind and activate SMAD transcriptional regulators. BMPR1B is receptor for BMP7/OP-1 as well as GDF5.
Synonyms
Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.
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 MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.
Background
Bone Morphogenetic Protein Receptor-1B Human Recombinant: A Key Regulator of Cellular Signaling in Development and Disease
Abstract:
Bone Morphogenetic Protein Receptor-1B (BMPR1B) human recombinant is a critical component of the bone morphogenetic protein (BMP) signaling pathway, governing cellular processes such as embryogenesis, tissue homeostasis, and disease progression. This research paper provides a comprehensive analysis of BMPR1B, including its characteristics, signaling mechanisms, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
The precise regulation of cellular signaling pathways is essential for proper development and tissue maintenance. BMPR1B, a key receptor in the BMP pathway, plays a crucial role in various biological processes. This paper explores the unique features of BMPR1B and presents novel approaches for its production and optimization, aiming to unravel its therapeutic potential in a wide range of developmental and disease contexts.
Characteristics and Signaling Mechanisms:
BMPR1B belongs to the serine/threonine kinase receptor family and is predominantly expressed in embryonic tissues, skeletal structures, and reproductive organs. Upon binding to BMP ligands, BMPR1B initiates downstream signaling cascades, including Smad-dependent and Smad-independent pathways. These pathways regulate gene expression, cellular proliferation, differentiation, and apoptosis, ultimately influencing tissue development and homeostasis.
Production of BMPR1B Human Recombinant:
Efficient production methodologies are pivotal for harnessing the therapeutic potential of BMPR1B human recombinant. Mammalian expression systems, such as Chinese hamster ovary (CHO) cells, have been widely employed to ensure proper folding and post-translational modifications of the receptor. Optimization strategies, including codon optimization and vector engineering, have been utilized to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1B recombinant protein.
Potential Therapeutic Applications:
BMPR1B human recombinant holds tremendous promise in the field of regenerative medicine and disease therapy. Dysregulation of the BMP signaling pathway has been implicated in various developmental disorders, including skeletal abnormalities and congenital malformations. Modulating BMPR1B activity using BMPR1B human recombinant may offer a targeted approach for promoting tissue regeneration and repair in these conditions. Furthermore, BMPR1B signaling is involved in several diseases, such as cancer and cardiovascular disorders, highlighting its potential as a therapeutic target for intervention.
Conclusion:
BMPR1B human recombinant represents a vital regulator in cellular signaling, with significant implications in development and disease. Optimizing production methodologies and expanding our understanding of its signaling mechanisms will further enhance its therapeutic potential. With its involvement in various biological processes and disease contexts, BMPR1B human recombinant emerges as a promising tool for regenerative medicine and targeted therapeutics.
What is the molecular weight/Mw of BMPR1B Protein?
BMPR1B Protein has a total Mw of 15.1kDa.

What is the source or expression system of BMPR1B Protein?
Escherichia Coli.

What is the Purity of BMPR1B Protein?
BMPR1B Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of BMPR1B Protein?
The biological functionality of BMPR1B Protein will be determined in the future.

What is the amino acid sequence of BMPR1B Protein?
MGSSHHHHHH SSGLVPRGSH MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.

What applications can BMPR1B Protein be used in?
BMPR1B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMPR1B Protein?
The endotoxin level is minimal, BMPR1B 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:

Galectin-2 Mouse Recombinant

Galectin-2, Gal-2, Lgals2, AI324147, 2200008F12Rik.

Product # :

CYT-019

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SDS-PAGE

Description

LGALS2 mouse Recombinant produced E. coli is a single polypeptide chain containing 153 amino acids (1-130) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LGALS2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha (LTA) with threat of myocardial infarction.
Synonyms
Galectin-2, Gal-2, Lgals2, AI324147, 2200008F12Rik.
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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
Background
What is the molecular weight/Mw of LGALS2 MOUSE Protein?
LGALS2 MOUSE Protein has a total Mw of 17.3kDa.

What is the source or expression system of LGALS2 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS2 MOUSE Protein?
LGALS2 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS2 MOUSE Protein?
The biological functionality of LGALS2 MOUSE Protein will be determined in the future.

What is the amino acid sequence of LGALS2 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.

What applications can LGALS2 MOUSE Protein be used in?
LGALS2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS2 MOUSE Protein?
The endotoxin level is minimal, LGALS2 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:

ADP-Ribosylation Factor-Like 5A Human Recombinant

ARL5, ARFLP5, ADP-ribosylation factor-like 5A.

Product # :

PRO-040

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Description

ARL5A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203amino acids (1-179a.a.) and having a molecular mass of 23.3kDa.ARL5A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ARL5A protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2mM PMSF and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
ARL5A is a member of the ARF family of GTP-binding proteins. ARFs are vital in eukaryotic vesicular trafficking pathways and have a crucial part in the activation of phospholipase D. Different from ARF family members, ARL5 is believed to lack ADP-ribosylation enhancing activity. ARL5A is developmentally regulated and has a role in nuclear dynamics and signaling cascades during embryonic development.
Synonyms
ARL5, ARFLP5, ADP-ribosylation factor-like 5A.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGILFT RIWRLFNHQE HKVIIVGLDN AGKTTILYQF SMNEVVHTSP TIGSNVEEIV INNTRFLMWD IGGQESLRSS WNTYYTNTEF VIVVVDSTDR ERISVTREEL YKMLAHEDLR KAGLLIFANK QDVKECMTVA EISQFLKLTS IKDHQWHIQA CCALTGEGLC QGLEWMMSRL KIR

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-7 Human Recombinant, His Tag

Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

Product # :

CYT-485

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Description

IL-7 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 152 amino acids fragment (26-177) and having a total molecular mass of 21.97 kDa with an amino-terminal hexahistidine tag. The IL-7 His-Tag protein is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin -7 His is supplied in 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells.
IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.
Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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:

Growth Hormone Mutant Zebrafish Recombinant

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

Product # :

CYT-709

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Somatotropin Zebrafish Mutant G113R Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.18 kDa. The Zebrafish Mutant G113R Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.5% NaHCO3 pH-8.

Purity

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

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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth-Hormone although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Zebrafish Mutant G113R in 0.4% NaHCO3 or water adjusted to pH-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Gln-Arg-Leu-Phe-Asn.

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:

Ciliary Neurotrophic Factor Receptor Human Recombinant

Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.

Product # :

CYT-883

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Description

CNTFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (23-342 a.a) and having a molecular mass of 38.1kDa. CNTFR is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Ciliary Neurotrophic Factor Receptor, also known as CNTFR is a member of the type I cytokine receptor family. CNTFR binds to CNTF. The alpha subunit provides the receptor specificity. Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
Synonyms
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha, Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.
Background
Unveiling the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Insights and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) holds a crucial role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper discusses the significance of Human Recombinant CNTFR, its production methods, and its potential applications in neurobiology and therapeutic interventions. The review sheds light on the pivotal role of CNTFR in neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, plays a pivotal role in transmitting CNTF-mediated signals to the cell. The availability of Human Recombinant CNTFR allows researchers to investigate its role in neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's involvement in modulating neuronal health and promoting regeneration makes it an essential component in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and initiate downstream signaling pathways. Activation of intracellular signaling cascades, such as JAK/STAT and MAPK, contributes to the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is produced through gene expression in suitable host cells, often employing bacterial or mammalian systems. Ensuring proper folding and post-translational modifications is essential to maintain its functionality and binding affinity for CNTF.
Therapeutic Applications:
The availability of Human Recombinant CNTFR offers potential therapeutic applications in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-mediated signaling presents opportunities to enhance neuronal survival and regeneration, ultimately improving patient outcomes.
Challenges and Future Directions:
While promising, challenges include optimizing the interaction between CNTFR and CNTF, ensuring efficient delivery to target tissues, and understanding potential off-target effects. Ongoing research is essential to unravel the complete mechanisms of CNTFR-mediated signaling and its implications for therapy.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor serves as a crucial tool in advancing our understanding of neuroprotection and regeneration. Its potential to modulate CNTF-mediated effects opens avenues for innovative therapeutic strategies targeting neurodegenerative disorders, exemplifying the intersection of molecular biology and clinical application.
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 38.1kDa.

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

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

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

What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MQRHSPQEAP HVQYERLGSD VTLPCGTANW DAAVTWRVNG TDLAPDLLNG SQLVLHGLEL GHSGLYACFH RDSWHLRHQV LLHVGLPPRE PVLSCRSNTY PKGFYCSWHL PTPTYIPNTF NVTVLHGSKI MVCEKDPALK NRCHIRYMHL FSTIKYKVSI SVSNALGHNA TAITFDEFTI VKPDPPENVV ARPVPSNPRR LEVTWQTPST WPDPESFPLK FFLRYRPLIL DQWQHVELSD GTAHTITDAY AGKEYIIQVA AKDNEIGTWS DWSVAAHATP WTEEPRHLTT EAQAAETTTS TTSSLAPPPT TKICDPGELG S.

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

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

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

Description:

Nuclear Factor Of Activated T Cells 2 Human Recombinant

Nuclear Factor Of Activated T Cells 2, Nuclear Factor Of Activated T-Cells, Cytoplasmic, Calcineurin-Dependent 2, Nuclear Factor Of Activated T-Cells 2, NFAT Pre-Existing Subunit, NF-ATc2, NFAT1, NFATP, Nuclear Factor Of Activated T-Cells, Preexisting Component , Nuclear Factor Of Activated T-Cells, Cytoplasmic 2, NFAT Transcription Complex, Preexisting Component, Preexisting Nuclear Factor Of Activated T-Cells 2, T Cell Transcription Factor NFAT1, T-Cell Transcription Factor NFAT1, NF-ATp, NFATc2.

Product # :

PRO-2535

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Description

NFATC2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 290 amino acids (396-678a.a.) and having a molecular mass of 33.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). NFATC2 is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NFATC2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) 40% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
NFATC2, also known as nuclear factor of activated T-cells 2, belongs to the nuclear factor of activated T cells family. NFATC2 takes a significant part in the course of T helper cell differentiation, activation, and effector function. Even though KO of an individual NFAT isoform in T cells directs to rather minor effects, T cells lacking for NFATC1 and 2 totally fail to produce T helper cell effector cytokines, for instance the interleukins IL-4 and IL-2. Moreover, NFATC2 is highly phosphorylated and kept in the cytoplasm. Next T cell receptor stimulation, dephosphorylation via calcium-activated calcineurin induces a conformational modification of NFATC2 which reveals a few nuclear localization sequences.
Synonyms
Nuclear Factor Of Activated T Cells 2, Nuclear Factor Of Activated T-Cells, Cytoplasmic, Calcineurin-Dependent 2, Nuclear Factor Of Activated T-Cells 2, NFAT Pre-Existing Subunit, NF-ATc2, NFAT1, NFATP, Nuclear Factor Of Activated T-Cells, Preexisting Component , Nuclear Factor Of Activated T-Cells, Cytoplasmic 2, NFAT Transcription Complex, Preexisting Component, Preexisting Nuclear Factor Of Activated T-Cells 2, T Cell Transcription Factor NFAT1, T-Cell Transcription Factor NFAT1, NF-ATp, NFATc2.
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
MPLEWPLSSQ SGSYELRIEV QPKPHHRAHY ETEGSRGAVK APTGGHPVVQ LHGYMENKPL GLQIFIGTAD ERILKPHAFY QVHRITGKTV TTTSYEKIVG NTKVLEIPLE PKNNMRATID CAGILKLRNA DIELRKGETD IGRKNTRVRL VFRVHIPESS GRIVSLQTAS NPIECSQRSA HELPMVERQD TDSCLVYGGQ QMILTGQNFT SESKVVFTEK TTDGQQIWEM EATVDKDKSQ PNMLFVEIPE YRNKHIRTPV KVNFYVINGK RKRSQPQHFT YHPVHHHHHH

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

Description:

IFN-Beta 1a Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.

Product # :

CYT-236

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Description

IFN-beta 1a Human Recombinant produced in CHO (Chinese Hamster Ovarian) cells is a single, glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 22500 Dalton.IFN-beta1a is purified by proprietary chromatographic techniques.

Source

CHO (Chinese Hamster Ovarian) cells.

Formulation

Lyophilized from a solution containing 91 mg Human Albumin, and 620 mg mannitol and 50mM Acetate acid pH 3.8.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 10⁶ IU/mg.

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Introduction
IFN-beta has antiviral, antibacterial and anticancer activities.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.
Stability
Lyophilized IFN-beta 1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Beta1a 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 IFN beta 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein has a total Mw of 22.5kDa.

What is the source or expression system of IFN BETA 1A HUMAN Protein?
CHO (Chinese Hamster Ovarian) cells.

What is the Purity of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN BETA 1A HUMAN Protein?
The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 106 IU/mg.

What is the amino acid sequence of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is composed from 166 amino acids.

What applications can IFN BETA 1A HUMAN Protein be used in?
IFN BETA 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN BETA 1A HUMAN Protein?
The endotoxin level is minimal, IFN BETA 1A 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:

Interleukin-21, Sf9 Human Recombinant

Interleukin-21 isoform 1, CVID11, IL-21, Za11.

Product # :

CYT-1072

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Description

IL21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 145 amino acids (30-162a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL21 is expressed with a 12 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL21 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Interleukin-21 isoform 1 or IL21, categorized as a T helper cytokine. IL21 is part of the regulation of immune responses, haematopoiesis and cell-mediated responses. IL21 has a key role in haematopoiesis and immune responses regulation, therefore can affect lymphocyte development. Activation of T cells leads to production of the IL21. The protein has a crucial role in the viral infections persistence.
Synonyms
Interleukin-21 isoform 1, CVID11, IL-21, Za11.
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
ADPEFMQGQD RHMIRMRQLI DIVDQLKNYV NDLVPEFLPA PEDVETNCEW SAFSCFQKAQ LKSANTGNNE RIINVSIKKL KRKPPSTNAG
RRQKHRLTCP SCDSYEKKPP KEFLERFKSL LQKMIHQHLS SRTHGSEDSH 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:

Interleukin-33 Rat Recombinant

Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.

Product # :

CYT-150

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Description

IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a molecular mass of 17.4kDa.The IL 33 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was determined by the dose-dependent stimulation of the proliferation of murine D10S cells is <0.5ng/ml, corresponding to a specific activity of >2,000,000units/mg.

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Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-33 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-33 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 IL-33 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SIQGTSLLTE SCALSTYNDQ SVSFVLENGC YVINVEDCGK NQEKDKVLLR YYESSFPAQS GDGVDGKKLM VNMSPIKDTD IWLNANDKDY SVELQKGDVS PPDQAFFVLH KKSSDFVSFE CKNLPGTYIG VKDNQLALVE ENDESCNNIM FKLSKM

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 B1, Mitochondrial Human Recombinant

Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.

Product # :

PRO-903

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Description

TFB1M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (28-346 a.a.) and having a molecular mass of 38.8kDa.TFB1M is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TFB1M protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TFB1M is a member of the methyltransferase superfamily. TFB1M is a dimethyltransferase which methylates mitochondrial 12S rRNA at the conserved stem loop. The TFB1M protein also is part of the basal mitochondrial transcription complex and is required for mitochondrial gene expression. TFB1M stimulates transcription independently of the methyltransferase activity.
Synonyms
Dimethyladenosine transferase 1 mitochondrial, Mitochondrial 12S rRNA dimethylase 1, Mitochondrial transcription factor B1, h-mtTFB, h-mtTFB1, hTFB1M, mtTFB1, S-adenosylmethionine-6-N'-N'-adenosyl(rRNA) dimethyltransferase 1, TFB1M, CGI-75, CGI75, mtTFB.
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 MQAAKQLSQN FLLDLRLTDK IVRKAGNLTN AYVYEVGPGP GGITRSILNA DVAELLVVEK DTRFIPGLQM LSDAAPGKLR IVHGDVLTFK VEKAFSESLK RPWEDDPPNV HIIGNLPFSV STPLIIKWLE NISCRDGPFV YGRTQMTLTF QKEVAERLAA NTGSKQRSRL SVMAQYLCNV RHIFTIPGQA FVPKPEVDVG VVHFTPLIQP KIEQPFKLVE KVVQNVFQFR RKYCHRGLRM LFPEAQRLES TGRLLELADI DPTLRPRQLS ISHFKSLCDV YRKMCDEDPQ LFAYNFREEL KRRKSKNEEK EEDDAENYRL.

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-6 Rat Recombinant

IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.

Product # :

CYT-388

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Description

Interleukin-6 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids and having a molecular mass of 21732 Dalton. The IL6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 0.02% TFA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ is less than 0.01 ng/ml as determined by dose-dependent stimulation of mouse 7TD1 cells.

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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 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-6 with 10mM HCl at a concentration of 0.1 mg/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 Met-Phe-Pro-Thr-Ser.
Background
Research Paper on Interleukin-6 Rat Recombinant
Abstract:
Exploring Interleukin-6 Rat Recombinant: This research paper provides an extensive description of Interleukin-6 (IL-6) Rat Recombinant, a vital cytokine in immunological studies. We delve into its molecular properties, significance in immune responses, and its synonyms, including DIF, TNFA, and TNFSF2. Join us as we uncover the potential applications of IL-6 Rat Recombinant in advancing our understanding of immune regulation.
Introduction:
Unraveling IL-6 Rat Recombinant: This paper introduces IL-6 Rat Recombinant, a valuable tool for investigating immune responses. As researchers, we are intrigued by its diverse functions and potential therapeutic implications.
An Extensive Description of IL-6 Rat Recombinant:
We present a comprehensive overview of IL-6 Rat Recombinant, focusing on its structural characteristics and involvement in immune signaling. This recombinant cytokine allows us to explore the complexities of IL-6 biology and its impact on immune system homeostasis.
Significance in Immune Responses:
Marvel at IL-6's pivotal role in orchestrating immune responses! As a crucial mediator between immune cells, IL-6 plays a critical role in regulating inflammation and immune cell activation. It also contributes to tissue repair and antibody production.
Interactions and Synonyms:
Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms enhances our comprehension of the interconnected cytokine network, contributing to a broader understanding of immune signaling.
Potential Applications in Immunological Research:
Explore the diverse applications of IL-6 Rat Recombinant in immunological research. From deciphering cellular responses to developing potential therapeutics, this recombinant cytokine serves as an indispensable tool for advancing our knowledge of the immune system. Researchers use it for in vitro studies, functional assays, and investigating disease pathogenesis.
Novel Insights and Therapeutic Implications:
Gain novel insights into the therapeutic implications of IL-6 Rat Recombinant. Understanding its role in disease pathogenesis may lead to the development of targeted therapies for various immune-related disorders. Clinical trials targeting IL-6 have shown promise in treating certain inflammatory conditions.
Conclusion:
Concluding our exploration of IL-6 Rat Recombinant, we recognize its significance in immunological research. The extensive description of this recombinant cytokine broadens our understanding of IL-6 biology and its potential applications in various fields. By utilizing this powerful tool, we strive to make significant advancements in immunology research for improved health outcomes.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.55 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 IL-6 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:

Interleukin-1 Alpha Porcine Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.

Product # :

CYT-396

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Description

Interleukin-1A Porice Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 158 amino acids and having a molecular mass of 18076 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

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-dependant stimulation of D10S cells is < 0.03 ng/ml.

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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha, IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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-1 alpha 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 Ser-Ala-Thr-Tyr-Ser.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.669 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 IL-1 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:

Interleukin-7 Mouse Recombinant

Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

Product # :

CYT-372

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Shipped at Room temp

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Description

Interleukin-7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4 and 2% trehalose.

Purity

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

Biological Activity

The ED₅₀was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2 ng/ml, corresponding to a specific activity of >5.0×10⁶ IU/mg.

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Introduction
Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells. IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.
Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ECHIKDKEGK AYESVLMISI DELDKMTGTD SNCPNNEPNF FRKHVCDDTK EAAFLNRAAR KLKQFLKMNI SEEFNVHLLT VSQGTQTLVN CTSKEEKNVK EQKKNDACFL KRLLREIKTC WNKILKGSI.

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:

CDKN2A Interacting Protein N-Terminal Like Human Recombinant

CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.

Product # :

PRO-1865

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Description

CDKN2AIPNL Human Recombinant produced in E. coli is. a single polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.6kDa. CDKN2AIPNL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CDKN2AIPNL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
CDKN2A Interacting Protein N-Terminal Like (CDKN2AIPNL) is a part of the CARF family.
Synonyms
CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.
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 MGSMVGGEAA AAVEELVSGV RQAADFAEQF RSYSESEKQW KARMEFILRH LPDYRDPPDG SGRLDQLLSL SMVWANHLFL GCSYNKDLLD KVMEMADGIE VEDLPQFTTR SELMKKHQS.

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:

Glucose-6-Phosphate Isomerase Human Recombinant, BioActive

Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.

Product # :

ENZ-1148

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Description

GPIHuman Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 578 amino acids (1-558) and having a molecular mass of 65.3 kDa.GPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GPI solution (1 mg/ml) contains 10% Glycerol, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 400unit/mg.It is defined by the increase of NADPH in absorbance at 340 nm, resulting from the reduction of NADP. 1 unit will convert 1.0 umole of D-Fructose 6-phosphate to D-glucose 6- phosphate per minute at pH 7.4 at 37˚C.

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Introduction
GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.
Synonyms
Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.
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 MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK QQREARVQ

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

Description:

Bone Morphogenetic protein-2, Mouse Anti-Human

BMP-2, BMP2A.

Product # :

ANT-183

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Source

The BMP-2 antibody was prepared by affinity chromatography from ascites of BALB/c mouseinoculated by a hybridoma cell that secreted anti- BMP-2 monoclonal antibodies.

Formulation

Samples are lyophilized in sterile PBS buffers.

Purity

Greater than 90%, analysed by reducing SDS-PAGE.

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Introduction
BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
Synonyms
BMP-2, BMP2A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
For long-term storage, keep aliquot samples at -70°C. Once reconstituted, samples are stable at 4°C for several weeks.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Applications
Applied in detections of antigen or antibody: ELISA or Western blot. For indirect ELISA, dilute antibody solution by 1: 250.
Type
Mouse Anti Human Monoclonal.

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:

LIGHT Human Recombinant

Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light

Product # :

CYT-1202

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Description

Recombinant Human LIGHT (74-240 aa) having a Mw of 23kDa was purified from E. coli.The Recombinant Human LIGHT is purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

TNFSF14 solution contains PBS & 25mM K2CO3.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light
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
DGPAGSWEQL IQERRSHEVN PAAHLTGANS SLTGSGGPLL WETQLGLAFL RGLSYHDGAL VVTKAGYYYI YSKVQLGGVG CPLGLASTIT HGLYKRTPRY PEELELLVSQ QSPCGRATSS SRVWWDSSFL GGVVHLEAGE KVVVRVLDER LVRLRDGTRS YFGAFMV

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:

Isocitrate Dehydrogenase 3 (NAD+) Gamma Human Recombinant

Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.

Product # :

ENZ-205

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Description

IDH3G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (40-393) and having a molecular mass of 41.1kDa.IDH3G is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IDH3G solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl, 5mM DTT and 2mM EDTA.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Isocitrate dehydrogenase [NAD] subunit gamma (IDH3G) mitochondrial is a member of the isocitrate and isopropylmalate dehydrogenases family. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. The IDH3G is a gamma subunit of one isozyme of isocitrate dehydrogenase which belongs to a distinct subclass, which utilizes NAD(+) as the electron acceptor, and is restricted to the mitochondrial matrix.
Synonyms
Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial, Isocitric dehydrogenase subunit gamma, NAD(+)-specific ICDH subunit gamma, IDH3G, H-IDHG.
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 MFSEQTIPPS AKYGGRHTVT MIPGDGIGPE LMLHVKSVFR HACVPVDFEE VHVSSNADEE DIRNAIMAIR RNRVALKGNI ETNHNLPPSH KSRNNILRTS LDLYANVIHC KSLPGVVTRH KDIDILIVRE NTEGEYSSLE HESVAGVVES LKIITKAKSL RIAEYAFKLA QESGRKKVTA VHKANIMKLG DGLFLQCCRE VAARYPQITF ENMIVDNTTM QLVSRPQQFD VMVMPNLYGN IVNNVCAGLV GGPGLVAGAN YGHVYAVFET ATRNTGKSIA NKNIANPTAT LLASCMMLDH LKLHSYATSI RKAVLASMDN ENMHTPDIGG QGTTSEAIQD VIRHIRVING RAVEA.

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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