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Description:

Inhibitor of Growth Family, Member 2 Human Recombinant

Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.

Product # :

PRO-1739

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Description

ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ING2 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
Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).
Synonyms
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
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 MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.

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 Receptor Antagonist Horse Recombinant

Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, IL1RN, IL1RA.

Product # :

CYT-010

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Description

Recombinant Horse Interleukin-1 Receptor Antagonist produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.4kDa. The IL-1RA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL-1RA was lyophilized from a 0.2µm filtered concentrated solution in PBS, 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 inhibiting IL-1α-dependent proliferation of murine D10.G4.1 helper T cells is less than 3.0 μg/ml, corresponding to a specific activity of > 333 IU/mg in the presence of 50 pg/ml rHuIL-1α.

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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
Synonyms
Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, IL1RN, IL1RA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-1RA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1RA 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 IL-1RA in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HPLGKRPCKM QAFRIWDVNQ KTFYMRNNQL VAGYLQESNT KLQEKIDVVP IEPDALFLGL HGRKLCLACV KSGDEIRFQL EAVNITDLSK NKEENKRFTF IRSNSGPTTS FESAACPGWF LCTAQEADRP VSLTNKPKES FMVTKFYLQE DQ.
Background
What is the molecular weight/Mw of IL1RA HORSE Protein?
IL1RA HORSE Protein has a total Mw of 17.4kDa.

What is the source or expression system of IL1RA HORSE Protein?
Escherichia Coli.

What is the Purity of IL1RA HORSE Protein?
IL1RA HORSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RA HORSE Protein?
The ED50 as determined by inhibiting IL-1α-dependent proliferation of murine D10.G4.1 helper T cells is less than 3.0 μg/ml, corresponding to a specific activity of > 333 IU/mg in the presence of 50 pg/ml rHuIL-1α.

What is the amino acid sequence of IL1RA HORSE Protein?
HPLGKRPCKM QAFRIWDVNQ KTFYMRNNQL VAGYLQESNT KLQEKIDVVP IEPDALFLGL HGRKLCLACV KSGDEIRFQL EAVNITDLSK NKEENKRFTF IRSNSGPTTS FESAACPGWF LCTAQEADRP VSLTNKPKES FMVTKFYLQE DQ.

What applications can IL1RA HORSE Protein be used in?
IL1RA HORSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RA HORSE Protein?
The endotoxin level is minimal. IL1RA HORSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RA HORSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL1RA HORSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Adiponectin Globular Recombinant, His Tag

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-277

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Description

Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).

Source

Escherichia Coli.

Formulation

Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.

Purity

Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.

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Introduction
Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Stability
For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.
Solubility
Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.
Amino Acid Sequence
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

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

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

Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK

Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

Product # :

PRO-2773

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Description

TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The TREM2 solution (1mg/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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Synonyms
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
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
HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.
Background
TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.
The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.
Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.
Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.
Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.

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:

F-Box Protein 2 Human Recombinant

F-box only protein 2, FBXO2, F-Box Protein 2, FBX2, FBG1, Fbs1, NFB42, OCP1.

Product # :

PRO-2017

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Description

FBXO2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 319 amino acids (1-296 a.a.) and having a molecular mass of 35.7kDa.FBXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FBXO2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
F-Box Protein 2 (FBXO2) is a part of the F-box protein family. The F-box proteins are one of the 4 subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which takes part in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes. FBXO2 belongs to the Fbxs class which contains either different protein-protein interaction modules or no recognizable motifs. FBXO2 is extremely similar to the rat neural F Box 42 kDa protein which is enriched in the nervous system and plays a role in maintaining neurons in a postmitotic state.
Synonyms
F-box only protein 2, FBXO2, F-Box Protein 2, FBX2, FBG1, Fbs1, NFB42, OCP1.
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 MGSMDGDGDP ESVGQPEEAS PEEQPEEASA EEERPEDQQE EEAAAAAAYL DELPEPLLLR VLAALPAAEL VQACRLVCLR WKELVDGAPL WLLKCQQEGL VPEGGVEEER DHWQQFYFLS KRRRNLLRNP CGEEDLEGWC DVEHGGDGWR VEELPGDSGV EFTHDESVKK YFASSFEWCR KAQVIDLQAE GYWEELLDTT QPAIVVKDWY SGRSDAGCLY ELTVKLLSEH ENVLAEFSSG QVAVPQDSDG GGWMEISHTF TDYGPGVRFV RFEHGGQDSV YWKGWFGARV TNSSVWVEP.

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:

Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta Human Recombinant

14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.

Product # :

PKA-254

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Description

YWHAQ Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 27 kDa. YWHAQ is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

YWHAQ solution containing 20mM Tris 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, ?, ?, ?, ?, ?, ? and ? that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.
Synonyms
14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.
Physical Appearance
Sterile filtered colorless solution.
Stability
YWHAQ Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWRVISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLKMKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYEILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN.

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:

Apoliporotein-H Bovine

Beta-2-glycoprotein 1, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH.

Product # :

PRO-1504

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Description

Bovine Apolipoprotein-H polypeptide is purified from fetal calf serum (FCS) by proprietary protein-chemical techniques, having an Mw of approximately 70kDa.

Source

Fetal calf serum (FCS).

Formulation

APOH protein solution is supplied in 16mM Tris-HCl pH-8.0, 280mM NaCl, 0.16mM AEBSF and 20% glycerol.

Purity

Greater than 70% as determined by SDS-PAGE.

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Introduction
Apolipoprotein H (APOH) attaches to numerous kinds of negatively charged substances for instance phospholipids, and dextran sulfate. APOH prevents activation of the intrinsic blood coagulation cascade by attaching to phospholipids on the surface of damaged cells. APOH expressed by the liver and secreted in the plasma.
Synonyms
Beta-2-glycoprotein 1, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH.
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. Avoid multiple 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:

Cytokeratin 14 Human Recombinant, His Tag

Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.

Product # :

PRO-941

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Description

KRT14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 492 amino acids (1-472 a.a.) and having a molecular mass of 53.8kDa.KRT14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

KRT14 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.
Synonyms
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
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 MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG GAYGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGTGLGGGF GGGFAGGDGL LVGSEKVTMQ NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK
DYSPYFKTIE DLRNKILTAT VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN
LEIELQSQLS MKASLENSLE ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN.

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:

Activin-B Human Recombinant, Active

Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

Product # :

CYT-057

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Description

Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana plant

Formulation

Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

Purity

Greater than 97.0% as determined by Analysis by SDS-PAGE.

Biological Activity

The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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Synonyms
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.
Background
An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active
1. Abstract
Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.
2. Introduction
The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.
3. Structure and Synthesis of Activin-B
Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.
4. Biological Functions of Activin-B
Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.
5. Activin-B in Regenerative Medicine
Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.
6. Activin-B and Reproductive Health
Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.
7. Activin-B in Cancer
Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.
8. Conclusion and Future Perspectives
Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.
What is the source or expression system of Activin B Protein?
Nicotinia

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

What is the Biological Activity of Activin B Protein?
The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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

What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

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 Human Recombinant, His Tag

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

Product # :

CYT-480

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Description

Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. The IL-1b His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1b His tag protein solution is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-1b is a potent pro-inflammatory cytokine produced by a wide variety of cell types including monocytes and macrophages. It displays a broad range of biological activity including activation of B and T cells in response to inflammation and the activation of endothelial 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 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
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
Background
What is the molecular weight/Mw of IL1B HUMAN, HIS Protein?
IL1B HUMAN, HIS Protein has a total Mw of 21.88kDa.

What is the source or expression system of IL1B HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL1B HUMAN, HIS Protein?
IL1B HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B HUMAN, HIS Protein?
The biological functionality of IL1B HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1B HUMAN, HIS Protein?
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.

What applications can IL1B HUMAN, HIS Protein be used in?
IL1B HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B HUMAN, HIS Protein?
The endotoxin level is minimal, IL1B HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

Description:

Rantes Human Recombinant (CCL5), His Tag

Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.

Product # :

CHM-361

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Description

Rantes Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 68 amino acids fragment (24-91) having a total molecular mass of 17.5kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.The Rantes His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.
Synonyms
Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.
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.
Background
What is the molecular weight/Mw of CCL5 HUMAN, HIS Protein?
CCL5 HUMAN, HIS Protein has a total Mw of 17.5kDa.

What is the source or expression system of CCL5 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL5 HUMAN, HIS Protein?
CCL5 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL5 HUMAN, HIS Protein?
The biological functionality of CCL5 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL5 HUMAN, HIS Protein?
CCL5 HUMAN, HIS Protein is composed from 68 amino acids.

What applications can CCL5 HUMAN, HIS Protein be used in?
CCL5 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL5 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL5 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL5 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL5 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Annexin A6 Human Recombinant

ANX6, ANXA6, Annexin-VI, Lipocortin-6, Lipocortin-VI, Annexin-6, CPB-II, Annexin A6, p68, p70, Protein III, Chromobindin-20, 67 kDa calelectrin, Calphobindin-II, CBP68.

Product # :

PRO-767

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Description

ANXA6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 693 amino acids (1-673 a.a.) and having a molecular mass of 78 kDa. ANXA6 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ANXA6 protein solution contains 20mM Tris-HCl, pH-8, 0.1M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
ANXA6 is part of the family of calcium-dependent membrane and phospholipid binding proteins. ANXA6 mediats the endosome aggregation and vesicle fusion in secreting epithelia during exocytosis. ANXA6 correlates with CD21. ANXA6 regulates the release of Ca(2+) from intracellular stores. ANXA6 is differentially expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period.
Synonyms
ANX6, ANXA6, Annexin-VI, Lipocortin-6, Lipocortin-VI, Annexin-6, CPB-II, Annexin A6, p68, p70, Protein III, Chromobindin-20, 67 kDa calelectrin, Calphobindin-II, CBP68.
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 MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR SNRQRQEVCQ SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE IKDAISGIGT DEKCLIEILA SRTNEQMHQL VAAYKDAYER DLEADIIGDT SGHFQKMLVV LLQGTREEDD VVSEDLVQQD VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA DFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ IRQTFKSHFG RDLMTDLKSE ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED YHKSLEDALS SDTSGHFRRI LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK TSLETRFMTI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD FLKALLALCG GED.

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:

S100 Calcium Binding Protein A9 Human Recombinant

Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.

Product # :

PRO-814

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Description

S100A9 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (1-114 a.a.) and having a molecular mass of 14.3kDa. S100A9 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

S100A9 Human solution containing 20mM Tris HCl pH-8, 0.1M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.
Synonyms
Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.
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
MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK KENKNEKVIE HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG PGHHHKPGLG EGTPLEHHHH HH.

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

Description:

Myostatin Human Recombinant, His Tag

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

Product # :

CYT-445

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Description

Total 152AA. M.W. 16.7kDa (calculated). N-terminal His-tag and spacer (43AA – highlighted). The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M acetate buffer, pH 4.5.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Myostatin (GDF-8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.
Synonyms
GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.
Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.

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:

Desert Hedgehog (C23II) Mouse Recombinant

Desert hedgehog protein, DHH, HHG-3, C78960.

Product # :

CYT-773

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Description

DHH (C23II) Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 20kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4, 1mM DTT and 0.05% Tween-80.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to induce alkaline phosphatase production by murine MC3T3-E1 cells is 5-20 µg/ml.

More Info

Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.
Synonyms
Desert hedgehog protein, DHH, HHG-3, C78960.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRGPVG RRRYVRKQLV PLLYKQFVPS MPERTLGASG PAEGRVTRGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH IHVSVKADNS LAVRAGG.

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-17F Human Recombinant, His Tag

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-762

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Description

IL 17F His Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (31-163) and having a molecular mass of 17.6kDa.IL 17F His is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL 17F His solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM_CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 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 MGSHMRKIPK VGHTFFQKPE SCPPVPGGSM KLDIGIINEN QRVSMSRNIE SRSTSPWNYT VTWDPNRYPS EVVQAQCRNL GCINAQGKED ISMNSVPIQQ ETLVVRRKHQ GCSVSFQLEK VLVTVGCTCV TPVIHHVQ

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-32 alpha Human Recombinant , His Tag

NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

Product # :

CYT-648

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Description

Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-131 a.a.) and having a molecular mass of 19.1 kDa. The IL-32 is fused to a 37 amino acid His Tag at N-terminus and purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The IL-32 His Tag protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of interferon gamma.
IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases.
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMCF PKVLSDDMKK LKARMHQAIE RFYDKMQNAE SGRGQVMSSL AELEDDFKEGYLETVAAYYE EQHPELTPLL EKERDGLRCR GNRSPVPDVE DPATEEPGES FCDKSYGAPR GDKEELTPQK CSEPQSSK.

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:

B-Cell Maturation Antigen Human Recombinant, His Tag

BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

Product # :

CYT-190

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Quantity :

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Description

TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (78-184 a.a) and having a molecular mass of 14.1kDa.TNFRSF17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFRSF17 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.

More Info

Introduction
TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.
Synonyms
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
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
MGSSHHHHHH SSGLVPRGSH MGSRKINSEP LKDEFKNTGS GLLGMANIDL EKSRTGDEII LPRGLEYTVE ECTCEDCIKS KPKVDSDHCF PLPAMEEGAT ILVTTKTNDY CKSLPAALSA TEIEKSISAR.

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:

Cytohesin 3 Human Recombinant

Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.

Product # :

PRO-1951

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Description

CYTH3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.7 kDa.CYTH3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CYTH3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.
Synonyms
Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.
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 MGSMDEDGGG EGGGVPEDLS LEEREELLDI RRRKKELIDD IERLKYEIAE VMTEIDNLTS VEESKTTQRN KQIAMGRKKF NMDPKKGIQF LIENDLLQSS PEDVAQFLYK GEGLNKTVIG DYLGERDEFN IKVLQAFVEL HEFADLNLVQ ALRQFLWSFR LPGEAQKIDR MMEAFASRYC LCNPGVFQST DTCYVLSFAI IMLNTSLHNH NVRDKPTAER FIAMNRGINE GGDLPEELLR NLYESIKNEP FKIPEDDGND LTHTFFNPDR EGWLLKLGGR VKTWKRRWFI LTDNCLYYFE YTTDKEPRGI IPLENLSIRE VEDPRKPNCF ELYNPSHKGQ VIKACKTEAD GRVVEGNHVV YRISAPSPEE KEEWMKSIKA SISRDPFYDM LATRKRRIAN KK.

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:

Twisted Gastrulation Protein Human Recombinant

Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.

Product # :

CYT-873

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Description

TWSG1 Human Recombinant (26-223) produced in CHO is a single, glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass ranging from 35-43kDa on SDS-PAGE due to glycosylation.The TWSG1 is purified by proprietary chromatographic techniques.

Source

CHO.

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 alkaline phosphatase production induced by rHuBMP-6 in mouse ATDC5 cells, is less than 16µg/ml.

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Introduction
Twisted gastrulation Protein (TSG) is a secreted, cysteine-rich protein which has a role in dorsal/ventral patterning in Drosophila and Xenopus by regulating BMP signaling. TSG functions as an agonist for BMP signaling by controlling the inhibitory actions of the BMP antagonist, Chordin/Sog, and the cleavage properties of the metalloprotease, xolloid/tolloid. TSG N-terminal domain binds BMP protein directly and displays BMP antagonist activity.
Synonyms
Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSG 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 TSG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CNKALCASDV SKCLIQELCQ CRPGEGNCSC CKECMLCLGA LWDECCDCVG MCNPRNYSDT PPTSKSTVEE LHEPIPSLFR ALTEGDTQLN WNIVSFPVAE ELSHHENLVS FLETVNQPHH QNVSVPSNNV HAPYSSDKEH MCTVVYFDDC MSIHQCKISC ESMGASKYRW FHNACCECIG PECIDYGSKT VKCMN CMF.

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-Alpha 2a Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.

Product # :

CYT-204

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Description

IFN Alpha Human 2a Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19241 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine.The Interferon-alpha-2a gene was obtained from human leukocytes.The IFNA2A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized without additives.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNA-2A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a 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 Interferon-alpha-2a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.
Background
What is the molecular weight/Mw of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein has a total Mw of 19.2kDa.

What is the source or expression system of IFN A 2A HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2A HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

What is the amino acid sequence of IFN A 2A HUMAN Protein?
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.

What applications can IFN A 2A HUMAN Protein be used in?
IFN A 2A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2A HUMAN Protein?
The endotoxin level is minimal, IFN A 2A HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.924 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IFN-a 2a 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:

Leptin Horse Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-504

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Description

Leptin Horse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

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

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin 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 Ala-Val-Pro-Ile-Gln.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.1 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 calibrated solution of Leptin Horse 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:

Fibroblast Growth Factor-basic Human Recombinant, Thermostable

HBGH-2, HBGF-2, FGF-2, FGF-b, HBGH2, HBGF2, FGF2, FGFb, FGF2 Thermostable, FGF-2 Thermostable.

Product # :

CYT-943

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Shipped at Room temp

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Description

FGF2 Thermostable is a stabilized form of FGF2 growth factor which enables a novel method to produce FGF2-dependent cell cultures more efficiently, having less media changes. FGF2 Thermostable can maintain its biological activity even after five days at 37°C. The increase in the stability of FGF2 in cell-culture enables a more homogenous, undifferentiated stem cell culture, while saving scientists crucial time and money, as frequent supplementation of FGF-basic and the everyday medium change is not necessary. Thermostable FGF-2 is a hyperstable protein. The Thermal stability of the protein is increased by 15°C compared to the wild-type FGF-2. Thermostable FGF-2 is more than 5-times prolonged half-life in human cell culture incubated at 37°C. The FGF-2 Thermostable protein is engineered with fully retained biological function and has no harmful stabilizing additives.Thermostable FGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a total calculated molecular mass is 17.2kDa.

Source

Escherichia Coli.

Formulation

FGF Basic Thermostable was lyophilized from 20mM Tris-HCl, 150mM NaCl & 5% Trehalose, pH-7.6.

Purity

Purity is greater than 95% as determined by SDS-PAGE.

Biological Activity

The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg

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Synonyms
FGF2 Thermostable, FGF-basic Thermostable.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thermostable FGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF2 Thermostable 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 FGF2 thermostable protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS
Background
Why Choose FGF2 Thermostable?
FGF2 can lose much of its activity after 1-2 days at 37°C due to unfolding and degradation. Thermostable FGF2 is engineered with amino acid substitutions that increase structural stability without significantly altering receptor binding or biological function.
What are the advantages of FGF2 Protein?
*Better maintenance of pluripotency markers
*Higher colony quality
*Faster expansion rates
*Reduced spontaneous differentiation
*Greater viability after passaging
What is the source or expression system of FGF2 Protein?
Escherichia Coli.

What is the Purity of FGF2 Protein?
FGF2 Protein is >95% pure as determined by SDS-PAGE.

What is the molecular weight / Mw of FGF2 Protein?
FGF2 Protein having a total Mw of 17.2kDa.

What is the Biological Activity of FGF2 Protein?
The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg.

What is the endotoxin level for FGF2 Protein?
The endotoxin level is minimal, FGF2 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of FGF2 Protein?
AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS

Is FGF2 Protein conjugated to a Tag?
FGF2 Protein is not conjugated to a tag.

What applications can FGF2 Protein be used in?
FGF2 Protein can probably be used in western blot, ELISA and Lateral Flow.

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-2 Receptor Gamma Human Recombinant

Interleukin 2 Receptor Gamma, IL-2 Receptor Subunit Gamma, IL-2R Subunit Gamma, CD132 Antigen, SCIDX1, IL-2RG, GammaC, SCIDX, IMD4, P64, Cytokine Receptor Common Subunit Gamma, Common Cytokine Receptor Gamma Chain, Interleukin-2 Receptor Subunit Gamma, Combined Immunodeficiency X-Linked, Severe Combined Immunodeficiency, CD132, CIDX, IL2RG.

Product # :

CYT-471

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Shipped with Ice Packs

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IL2RG Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (23-262 a.a.) and having a molecular mass of 29kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).IL2RG is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL2RG protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 80.0% by SDS-PAGE.

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Introduction
Interleukin-2 Receptor Gamma (IL2RG) is a cytokine receptor sub-unit which is common to the receptor complexes for at least six different interleukin receptors. IL2RG is located on the surface of immature blood-forming cells in bone marrow. One end of the IL2RG protein resides outside of the cell where it binds to cytokines and the other end of the IL2RG protein resides in the interior of the cell where it transmits signals to the cell's nucleus. IL2RG teams up with other proteins to direct blood-forming cells to form lymphocytes. In addition, IL2RG directs the growth and maturation of lymphocyte subtypes, which kill viruses, make antibodies, and help regulate the entire immune system.
Synonyms
Interleukin 2 Receptor Gamma, IL-2 Receptor Subunit Gamma, IL-2R Subunit Gamma, CD132 Antigen, SCIDX1, IL-2RG, GammaC, SCIDX, IMD4, P64, Cytokine Receptor Common Subunit Gamma, Common Cytokine Receptor Gamma Chain, Interleukin-2 Receptor Subunit Gamma, Combined Immunodeficiency X-Linked, Severe Combined Immunodeficiency, CD132, CIDX, IL2RG.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
LNTTILTPNG NEDTTADFFL TTMPTDSLSV STLPLPEVQC FVFNVEYMNC TWNSSSEPQP TNLTLHYWYK NSDNDKVQKC SHYLFSEEIT SGCQLQKKEI HLYQTFVVQL QDPREPRRQA TQMLKLQNLV IPWAPENLTL HKLSESQLEL NWNNRFLNHC LEHLVQYRTD WDHSWTEQSV DYRHKFSLPS VDGQKRYTFR VRSRFNPLCG SAQHWSEWSH PIHWGSNTSK ENPFLFALEA HHHHHH.
Background
What is the molecular weight/Mw of IL2 RG HUMAN Protein?
IL2 RG HUMAN Protein has a total Mw of 29kDa.

What is the source or expression system of IL2 RG HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL2 RG HUMAN Protein?
IL2 RG HUMAN Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of IL2 RG HUMAN Protein?
The biological functionality of IL2 RG HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL2 RG HUMAN Protein?
LNTTILTPNG NEDTTADFFL TTMPTDSLSV STLPLPEVQC FVFNVEYMNC TWNSSSEPQP TNLTLHYWYK NSDNDKVQKC SHYLFSEEIT SGCQLQKKEI HLYQTFVVQL QDPREPRRQA TQMLKLQNLV IPWAPENLTL HKLSESQLEL NWNNRFLNHC LEHLVQYRTD WDHSWTEQSV DYRHKFSLPS VDGQKRYTFR VRSRFNPLCG SAQHWSEWSH PIHWGSNTSK ENPFLFALEA HHHHHH.

What applications can IL2 RG HUMAN Protein be used in?
IL2 RG HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL2 RG HUMAN Protein?
The endotoxin level is minimal, IL2 RG HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL2 RG HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL2 RG HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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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