Search: 1000 results found for "Anti Human Cytokine"

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.

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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:

Apolipoprotein E4 Human Recombinant

Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.

Product # :

CYT-968

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Description

Apolipoprotein E4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 299 amino acids and having a molecular mass of 34.4kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 20mM PBS, pH7.8 and 5% trehalose.

Purity

Greater than 95% as determined by:

(a) Analysis by RP-HPLC.

(b) Analysis by SDS-PAGE.

Biological Activity

When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

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Introduction
Apolipoprotein E (APOE) is a chylomicron lipoprotein which is essential for the metabolism of lipoproteins and lipid transport. The APOE gene has 3 alleles, designated APOE2, APOE3, and APOE4. The APOE allelic proteins differ by only one or two amino acids, however have different biological structures and functions. APOE3 is the most common and neutral allele. The APOE4 allele is linked with an increased risk for Alzheimer's Disease (AD) and coronary artery disease (CAD). The APOE4 protein morphology decreases the ability of APOE4 to clear beta-amyloid protein from the brain, resulting in AD progression. The APOE2 allele is linked with type III hyperlipoproteinemia, which is characterized by defects in the clearance of plasma lipoproteins, however APOE2 may have a protective effect against AD.
Synonyms
Apolipoprotein E, APO-E, Alzheimer Disease 2 (APOE*E4-Associated, Late Onset), Apolipoprotein E3, LDLCQ5, LPG, AD2, APOE.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized APOE4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution APOE4 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 APOE4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.
Background
What is the molecular weight/Mw of APOE4 Protein?
APOE4 Protein has a total Mw of 34.4kDa.

What is the source or expression system of APOE4 Protein?
Escherichia Coli.

What is the Purity of APOE4 Protein?
APOE4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of APOE4 Protein?
When Recombinant Human ApoE4 is immobilized at 1µg/mL (100 µl/well), the concentration of recombinant mouse VLDLR that produces 50% of the optimal binding response is found to be approximately 0.075 - 0.375 µg/mL.

What is the amino acid sequence of APOE4 Protein?
KVEQAVETEP EPELRQQTEW QSGQRWELAL GRFWDYLRWV QTLSEQVQEE LLSSQVTQEL RALMDETMKE LKAYKSELEE QLTPVAEETR ARLSKELQAA QARLGADMED VRGRLVQYRG EVQAMLGQST EELRVRLASH LRKLRKRLLR DADDLQKRLA VYQAGAREGA ERGLSAIRER LGPLVEQGRV RAATVGSLAG QPLQERAQAW GERLRARMEE MGSRTRDRLD EVKEQVAEVR AKLEEQAQQI RLQAEAFQAR LKSWFEPLVE DMQRQWAGLV EKVQAAVGTS AAPVPSDNH.

What applications can APOE4 Protein be used in?
APOE4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOE4 Protein?
The endotoxin level is minimal, APOE4 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:

IL-6 Receptor Beta Mouse Recombinant

IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.

Product # :

CYT-918

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Description

IL6R produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 603 amino acids (23-617a.a.) and having a molecular mass of 67.7kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).IL6R is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IL6R protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.
Synonyms
IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.
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
QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.
Background
Research Paper on IL-6 Receptor Beta Mouse Recombinant
Abstract:
The IL-6 Receptor Beta Mouse Recombinant stands as a pivotal player in deciphering the intricate realm of immune modulation. This research paper offers an in-depth exploration of its molecular intricacies and its profound implications in immunological research. By delving into its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its role in shaping immune responses.
Introduction:
The IL-6 Receptor Beta Mouse Recombinant has emerged as a central focus in immunological investigations. This paper aims to provide a comprehensive understanding of its molecular attributes and its influence on immune mechanisms.
Molecular Insights and Signaling Proficiency:
Examining the molecular architecture of IL-6 Receptor Beta Mouse Recombinant, we uncover its critical role in transducing IL-6 signals. Its intricate interactions and signaling proficiency contribute to precise immune responses.
Influencing Immune Responses:
IL-6, a key cytokine, exerts remarkable effects on immune cell activation and inflammation. IL-6 Receptor Beta Mouse Recombinant serves as an essential component in the IL-6 signaling pathway, influencing immune outcomes.
Synonyms and Network Connections:
Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, deepens our comprehension of cytokine-mediated signaling networks. The intricate interplay between IL-6 Receptor Beta Mouse Recombinant and these molecules shapes immune dynamics.
Potential Therapeutic and Research Applications:
IL-6 Receptor Beta Mouse Recombinant transcends the boundaries of laboratory research. Its potential as a therapeutic target for immune-related disorders and its utility in deciphering immune responses offer promising avenues for clinical applications.
Clinical Relevance and Future Prospects:
The clinical relevance of IL-6 Receptor Beta Mouse Recombinant is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies to modulate immune-related conditions.
Conclusion:
In the intricate tapestry of immunology, IL-6 Receptor Beta Mouse Recombinant emerges as a central player in orchestrating immune responses. Its molecular intricacies, pivotal functions, and potential therapeutic implications position it as a cornerstone in understanding immune regulation and developing innovative interventions.
What is the molecular weight/Mw of IL6R MOUSE Protein?
IL6R MOUSE Protein has a total Mw of 67.7kDa.

What is the source or expression system of IL6R MOUSE Protein?
Sf9, Insect cells.

What is the Purity of IL6R MOUSE Protein?
IL6R MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6R MOUSE Protein?
QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.

What is the amino acid sequence of IL6R MOUSE Protein?
IL6R MOUSE Protein is composed from XX amino acids.

What applications can IL6R MOUSE Protein be used in?
IL6R MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6R MOUSE Protein?
The endotoxin level is minimal, IL6R MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6R MOUSE 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 IL6R MOUSE?
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:

Apolipoprotein A-V Human Recombinant

Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.

Product # :

CYT-767

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Description

APOA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (24-366 a.a.) and having a molecular mass of 41.3kDa.APOA5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APOA5 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

More Info

Synonyms
Apolipoprotein A-V, Apo-AV, ApoA-V, Apolipoprotein A5, Regeneration-associated protein 3, APOA5, RAP3, APOAV.
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 MGSRKGFWDY FSQTSGDKGR VEQIHQQKMA REPATLKDSL EQDLNNMNKF LEKLRPLSGS EAPRLPQDPV GMRRQLQEEL EEVKARLQPY MAEAHELVGW NLEGLRQQLK PYTMDLMEQV ALRVQELQEQ LRVVGEDTKA QLLGGVDEAW ALLQGLQSRV VHHTGRFKEL FHPYAESLVS GIGRHVQELH RSVAPHAPAS PARLSRCVQV LSRKLTLKAK ALHARIQQNL DQLREELSRA FAGTGTEEGA GPDPQMLSEE VRQRLQAFRQ DTYLQIAAFT RAIDQETEEV QQQLAPPPPG HSAFAPEFQQ TDSGKVLSKL QARLDDLWED ITHSLHDQGH SHLGDP.
Background
Apolipoprotein A-V Human Recombinant: Unleashing the Power of Lipid Regulation
Abstract:

Apolipoprotein A-V (ApoA-V), a fascinating player in the intricate world of lipid metabolism, has emerged as a promising therapeutic target for lipid disorders. Produced primarily in the liver, ApoA-V exerts a profound influence on triglyceride metabolism. Dysregulation of ApoA-V has been implicated in various lipid-related disorders, including hypertriglyceridemia and cardiovascular diseases (CVDs). This research paper offers a concise yet comprehensive exploration of ApoA-V human recombinant, shedding light on its physiological functions, production methods, and potential therapeutic applications.
Introduction:

In the face of the soaring global burden of lipid disorders and cardiovascular ailments, novel therapeutic approaches are urgently needed. Apolipoproteins, the guardians of lipid transport, present promising targets for intervention. Among them, ApoA-V, a master regulator of triglyceride metabolism, holds great promise.
Structure and Function of Apolipoprotein A-V:

ApoA-V boasts an elegant molecular architecture, comprising specific domains that enable its interaction with lipoproteins engaged in lipid transport. Through its intricate mechanisms, ApoA-V fine-tunes triglyceride levels by modulating lipoprotein lipase activity and enhancing the clearance of triglyceride-rich lipoproteins.
Genetic Variations and Lipid Disorders:

Exploring the fascinating realm of genetics has uncovered ApoA-V gene polymorphisms linked to dyslipidemia, including hypertriglyceridemia. These genetic variations influence ApoA-V expression and function, thereby contributing to the development of lipid disorders and heightened cardiovascular risk.
Production of Apolipoprotein A-V Human Recombinant:

Harnessing the power of biotechnology, scientists have devised various expression systems, encompassing mammalian cells and bacteria, to produce recombinant ApoA-V. These techniques enable large-scale production, purification, and meticulous characterization of the recombinant protein, opening doors to potential therapeutic applications.
Therapeutic Applications of Apolipoprotein A-V Human Recombinant:

The prospect of targeting ApoA-V beckons as a promising avenue for managing lipid disorders, particularly hypertriglyceridemia. By manipulating ApoA-V expression or function, it becomes possible to reduce triglyceride levels, improve lipid profiles, and mitigate the risk of cardiovascular complications.
Conclusion:

Apolipoprotein A-V human recombinant represents a beacon of hope in the quest to conquer lipid disorders. Understanding the intricate interplay between ApoA-V's structure, function, and genetic variations offers profound insights into its potential role in personalized medicine. Unleashing the full therapeutic potential of ApoA-V human recombinant requires further scientific exploration and clinical studies, paving the way for effective interventions in lipid-related disorders.
What is the molecular weight/Mw of APOA5 Protein?
APOA5 Protein has a total Mw of 41.3kDa.

What is the source or expression system of APOA5 Protein?
Escherichia Coli.

What is the Purity of APOA5 Protein?
APOA5 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of APOA5 Protein?
The biological functionality of APOA5 Protein will be determined in the future.

What is the amino acid sequence of APOA5 Protein?
MGSSHHHHHH SSGLVPRGSH MGSRKGFWDY FSQTSGDKGR VEQIHQQKMA REPATLKDSL EQDLNNMNKF LEKLRPLSGS EAPRLPQDPV GMRRQLQEEL EEVKARLQPY MAEAHELVGW NLEGLRQQLK PYTMDLMEQV ALRVQELQEQ LRVVGEDTKA QLLGGVDEAW ALLQGLQSRV VHHTGRFKEL FHPYAESLVS GIGRHVQELH RSVAPHAPAS PARLSRCVQV LSRKLTLKAK ALHARIQQNL DQLREELSRA FAGTGTEEGA GPDPQMLSEE VRQRLQAFRQ DTYLQIAAFT RAIDQETEEV QQQLAPPPPG HSAFAPEFQQ TDSGKVLSKL QARLDDLWED ITHSLHDQGH SHLGDP.

What applications can APOA5 Protein be used in?
APOA5 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for APOA5 Protein?
The endotoxin level is minimal, APOA5 Protein was purified using conventional chromatography techniques

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

Description:

Bone Morphogenetic protein-2 Human Recombinant, HEK

BMP-2, BMP2A.

Product # :

CYT-080

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Shipped at Room temp

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Description

BMP-2 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 28kDa due to glycosylation. The BMP2 is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The BMP2 was lyophilized from 0.67mg/ml in 2xPBS + 6% ethanol.

Purity

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

Biological Activity

The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.

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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
Lyophilized BMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BMP-2 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.
Amino Acid Sequence
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.
Background
What is the molecular weight/Mw of BMP2 Protein?
BMP2 Protein has a total Mw of 28kDa.

What is the source or expression system of BMP2 Protein?
Hek.

What is the Purity of BMP2 Protein?
BMP2 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP2 Protein?
The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.

What is the amino acid sequence of BMP2 Protein?
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.

What applications can BMP2 Protein be used in?
BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP2 Protein?
The endotoxin level is minimal, BMP2 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-2 Canine Recombinant

Interleukin-2, IL-2, T-cell growth factor, TCGF.

Product # :

CYT-1096

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-2 Canine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 136 amino acids and having a molecular mass of 15.6kDa. IL-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 20 mM sodium bicarbonate, pH 8.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by CTLL-2 cell proliferation is <5ng/ml corresponding to a specific activity which is ≥ 2.0 x 10^5 units/mg.

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Introduction
IL2 is a secreted cytokine that is essential for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 and interleukin 7. The expression of IL2in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the exact expression of a single gene.
Synonyms
Interleukin-2, IL-2, T-cell growth factor, TCGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-2 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-2 in Sterile 10 mM sodium bicarbonate, pH 8.5 at 0.1 mg/mL, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPITSSSTK ETEQQMEQLL LDLQLLLNGV NNYENPQLSR MLTFKFYTPK KATEFTHLQC LAEELKNLEE VLGLPQSKNV HLTDTKELIS NMNVTLLKLK GSETSYNCEY DDETATITEF LNKWITFSQS IFSTLT.
Background
What is the molecular weight/Mw of IL 2 CANINE Protein?
IL 2 CANINE Protein has a total Mw of 15.6kDa.
What is the source or expression system of IL 2 CANINE Protein?
Escherichia Coli.

What is the Purity of IL 2 CANINE Protein?
IL 2 CANINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 CANINE Protein?
The ED50, as determined by CTLL-2 cell proliferation is <5ng/ml corresponding to a specific activity which is ≥ 2.0 x 10^5 units/mg.

What is the amino acid sequence of IL 2 CANINE Protein?
MAPITSSSTK ETEQQMEQLL LDLQLLLNGV NNYENPQLSR MLTFKFYTPK KATEFTHLQC LAEELKNLEE VLGLPQSKNV HLTDTKELIS NMNVTLLKLK GSETSYNCEY DDETATITEF LNKWITFSQS IFSTLT.

What applications can IL 2 CANINE Protein be used in?
IL 2 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 CANINE Protein?
The endotoxin level is minimal, IL 2 CANINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 CANINE 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 IL 2 CANINE?
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:

LAG-1 Human Recombinant (CCL4L1)

C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.

Product # :

CHM-018

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Description

LAG-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa.The CCL4L1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LAG-1 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 ED₅₀as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

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Introduction
CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.
Synonyms
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LAG-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4L1 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 LAG-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.
Background
What is the molecular weight/Mw of CCL4L1 HUMAN Protein?
CCL4L1 HUMAN Protein has a total Mw of 7.8kDa.

What is the source or expression system of CCL4L1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL4L1 HUMAN Protein?
CCL4L1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL4L1 HUMAN Protein?
The ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

What is the amino acid sequence of CCL4L1 HUMAN Protein?
APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.

What applications can CCL4L1 HUMAN Protein be used in?
CCL4L1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL4L1 HUMAN Protein?
The endotoxin level is minimal, CCL4L1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL4L1 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 CCL4L1 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.

Description:

B-type Natriuretic Peptide Human Recombinant

NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

Product # :

CYT-327

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Description

B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

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Introduction
Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.
Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized B-type Natriuretic Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NPPB should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized B-type Natriuretic Peptide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.
Background
What is the molecular weight / Mw of BNP Protein?
BNP Protein has a total Mw of 3.5kDa.

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

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

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

What is the amino acid sequence of BNP Protein?
SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

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

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

Chitinase 3-Like 2, Mouse Anti Human

Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.

Product # :

ANT-703

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Formulation

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

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Introduction
Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity, but not heparin.
Synonyms
Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CHI3L2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CHI3L2 amino acids 27-390 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT2B5AT.
Applications
CHI3L2 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
CHI3L2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

Description:

CD3, Mouse Anti-Human

Product # :

ANT-144

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
CD3 has four peptide chains (gamma, delta, epsilon and zeta) that form CD3. Defects in CD3 are associated with T cell immunodeficiency CD3 complex mediates signal transduction.
Solubility
Reconstitute with of H2O. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Purified human PBL T cells.
Ig Subclass
Mouse IgG2a.
Clone
hCD3.
Applications
Blocking, staining and activating antibody. For staining, use 10µl/1,000,000 cells. Titer for blocking and activating T cells should be determined by the investigator.
Available Conjugates
This antibody is also available conjugated to biotin and FITC.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
Lyophilized: store at 4C. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
Purification Method
Ion exchange column.

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:

Interferon Alpha And Beta Receptor Mouse Recombinant

IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.

Product # :

CYT-994

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Description

IFNAR1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (27-429a.a) and having a molecular mass of 46.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IFNAR1 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IFNAR1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interferon Alpha And Beta Receptor, also known IFNAR1, belongs to the class II cytokine receptor family. IFNAR1 protein forms one of the two chains of a receptor for interferons alpha as well as beta. IFNAR1 binds and activates the receptor which stimulates Janus protein kinases, which in turn phosphorylate some proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also functions as an antiviral factor.
Synonyms
IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.
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
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H
Background
What is the molecular weight/Mw of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein has a total Mw of 46.8kDa.

What is the source or expression system of IFNAR1 MOUSE Protein?
Sf9, Baculovirus cells.
What is the Purity of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNAR1 MOUSE Protein?
The biological functionality of IFNAR1 MOUSE Protein will be determined in the future.

What is the amino acid sequence of IFNAR1 MOUSE Protein?
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H

What applications can IFNAR1 MOUSE Protein be used in?
IFNAR1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNAR1 MOUSE Protein?
The endotoxin level is minimal, IFNAR1 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:

Thrombopoietin Mouse Recombinant, HEK

Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.

Product # :

CYT-1157

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Description

TPO Mouse Recombinant produced in HEK293 cells is a single, non-glycosylated polypeptide chain containing 341 amino acids ( 22-356 a.a) and having a molecular mass of 36.4kDa. TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293.

Formulation

TPO protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 range ≤4ng/ml.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

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Introduction
Thrombopoietin or TPO or MGDF, is a protein (glycoprotein hormone) that can be found in the liver and kidney tissues. TPO regulates the creation of platelets. The protein enhances the production & differentiation of cells such as megakaryocytes that are part of the bone marrow cells that secretes a wide number of platelets. The cellular development process that ends up in the production of platelet calls (Megakaryocytopoiesis). Humoral growth factor is needed for the megakaryocyte proliferation & maturation of megakaryocyte, not apart from thrombopoiesis.
Synonyms
Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 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
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKFPNRTSG LLETNFSVTA RTAGPGLLSR LQGFRVKITP GQLNQTSRSP VQISGYLNRT HGPVNGTHGL FAGTSLQTLE ASDISPGAFN KGSLAFNLQG GLPPSPSLAP DGHTPFPPSP ALPTTHGSPP QLHPLFPDPS TTMPNSTAPH PVTMYPHPRN LSQETHHHHH H.

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

Description:

Toll-Interleukin 1 Receptor (TIR) Domain Containing Adaptor Protein Human Recombinant

Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.

Product # :

PRO-1181

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Description

TIRAP Human Recombinant produced in E. coli is a single polypeptide chain containing 244 amino acids (1-221) and having a molecular mass of 26.3 kDa.TIRAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TIRAP solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.
Synonyms
Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASSTSL PAPGSRPKKP LGKMADWFRQ TLLKKPKKRP NSPESTSSDA SQPTSQDSPL PPSLSSVTSP SLPPTHASDS GSSRWSKDYD VCVCHSEEDL VAAQDLVSYL EGSTASLRCF LQLRDATPGG AIVSELCQAL SSSHCRVLLI TPGFLQDPWC KYQMLQALTE APGAEGCTIP LLSGLSRAAY PPELRFMYYV DGRGPDGGFR QVKEAVMRYL QTLS

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:

RELM-Gamma Mouse Recombinant, His Tag

Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

Product # :

CYT-455

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Shipped at Room temp

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Description

RELM-gamma Mouse Recombinant is a His -Tagged Fusion Protein having a molecular weight of 11 kDa containing 86 amino acid residues of the RELM-gamma Mouse and 16 additional amino acid residues – HisTag (underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
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.The lyophilized protein remains stable until the expiry date when stored at -20°C.
Solubility
It is recommended to add 0.1M Acetate buffer pH4 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MRGSHHHHHH GMASHMTLES IVEKKVKELL ANRDDCPSTV TKTFSCTSIT ASGRLASCPS GMTVTGCACG YGCGSWDIRD GNTCHCQCST MDWATARCCQ LA.

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:

Leukemia Inhibitory Factor Receptor Alpha Mouse Recombinant

Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.

Product # :

CYT-1170

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Description

LIFR Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 794 amino acids (44-828 aa) and having a molecular mass of 89.6kDa.LIFR is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit proliferation using TF-1 human erythroleukemic cells. The ED50 range ≤ 1ug/ml with Mouse LIF.

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Introduction
Leukemia Inhibitory Factor Receptor Alpha or LIFR is a protein, part of the Interleukin-6 receptor group of proteins. As such, LIFR acts as a mediator for various proteins (IL-6, IL-11, IL-27, Oncostatin M etc). LIFR has many functions as a cytokine, he has an affect on the cell proliferation, differentiation and survival in the different stages of life. In different types of breast cancer LIFR is down regulated, and as such, can be used as a prognostic tool.
Synonyms
Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.
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
ADPLKRGVQD LKCTTNNMRV WDCTWPAPLG VSPGTVKDIC IKDRFHSCHP LETTNVKIPA LSPGDHEVTI NYLNGFQSKF TLNEKDVSLI PETPEILDLS ADFFTSSLLL KWNDRGSALP HPSNATWEIK VLQNPRTEPV ALVLLNTMLS GKDTVQHWNW TSDLPLQCAT HSVSIRWHID SPHFSGYKEW SDWSPLKNIS WIRNTETNVF PQDKVVLAGS NMTICCMSPT KVLSGQIGNT LRPLIHLYGQ TVAIHILNIP VSENSGTNII FITDDDVYGT VVFAGYPPDV PQKLSCETHD LKEIICSWNP GRITGLVGPR NTEYTLFESI SGKSAVFHRI EGLTNETYRL GVQMHPGQEI HNFTLTGRNP LGQAQSAVVI NVTERVAPHD PTSLKVKDIN STVVTFSWYL PGNFTKINLL CQIEICKANS KKEVRNATIR GAEDSTYHVA VDKLNPYTAY TFRVRCSSKT FWKWSRWSDE KRHLTTEATP SKGPDTWREW SSDGKNLIVY WKPLPINEAN GKILSYNVSC SLNEETQSVL EIFDPQHRAE IQLSKNDYII SVVARNSAGS SPPSKIASME IPNDDITVEQ AVGLGNRIFL TWRHDPNMTC DYVIKWCNSS RSEPCLLDWR KVPSNSTETV IESDQFQPGV RYNFYLYGCT NQGYQLLRSI IGYVEELAPI VAPNFTVEDT SADSILVKWD DIPVEELRGF LRGYLFYFQK GERDTPKTRS LEPHHSDIKL KNITDISQKT LRIADLQGKT SYHLVLRAYT HGGLGPEKSM FVVTKENSHH HHHH.

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

Description:

Follistatin Human Recombinant, Sf9

Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.

Product # :

CYT-865

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sds-page
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Description

FST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (30-317a.a.) and having a molecular mass of 32.5kDa.FST is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FST protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.
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
MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN, SF9 Protein?
FOLLISTATIN HUMAN, SF9 Protein has a total Mw of 32.5kDa.

What is the source or expression system of FOLLISTATIN HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of FOLLISTATIN HUMAN, SF9 Protein?
FOLLISTATIN HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FOLLISTATIN HUMAN, SF9 Protein?
The biological functionality of FOLLISTATIN HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of FOLLISTATIN HUMAN, SF9 Protein?
MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH.

What applications can FOLLISTATIN HUMAN, SF9 Protein be used in?
FOLLISTATIN HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FOLLISTATIN HUMAN, SF9 Protein?
The endotoxin level is minimal, FOLLISTATIN HUMAN, SF9 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:

Serum Amyloid A (APO-SAA) Feline Recombinant

Product # :

CYT-1221

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Description

SAA Feline produced in E.coli is a single, non-glycosylated polypeptide chain (1-111 a.a) containing 121 a.a and having a molecular mass of 13,838 Dalton. SAA s fused with a 10 amino acids His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SAA was lyophilized from 0.01M HCl (pH 2.0).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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 SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
In response to infection, injury, or inflammation, SAA levels rapidly rise in the bloodstream. Acting as a chemoattractant, SAA recruits immune cells to the site of injury, facilitating the innate immune response. Additionally, SAA modulates the activities of immune cells, influencing cytokine production and phagocytosis. These immunomodulatory functions highlight SAA's significance in shaping the immune landscape during inflammatory events. SAA participates in lipid metabolism by interacting with HDL particles. In the acute-phase response, SAA displaces apolipoprotein A1 from HDL, transforming it into a pro-inflammatory particle. This alteration in HDL composition affects its cardioprotective functions, potentially contributing to atherosclerosis and cardiovascular diseases. Understanding these interactions is crucial for deciphering the intricate relationship between inflammation and cardiovascular health.

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:

Gankyrin, Mouse Anti Human

26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.

Product # :

ANT-609

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Formulation

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

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Introduction
Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.
Synonyms
26S proteasome non-ATPase regulatory subunit 10, 26S proteasome regulatory subunit p28, Gankyrin, PSMD10, p28, dJ889N15.2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human PSMD10 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PSMD10 protein 1-226 amino acids purified from E.coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT1F4AT.
Applications
PSMD10 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
PSMD10 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

Description:

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:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

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

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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:

Resistin Rat Recombinant, His Tag

Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

Product # :

CYT-458

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Description

Resistin Rat Recombinant is manufactured with N-terminal fusion of His tag. Resistin Rat Recombinant His-Tagged Fusion Protein is an 11.9 kDa protein containing 94 amino acid residues of the Resistin Rat and 16 additional amino acid residues – His Tag (underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris pH 8.0.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Mouse resistin is expressed as a 114 amino acid prepeptide; its hydrofobic Nterminal 20 amino acid signal peptide is cleaved before its secretion. Mouse resistin circulates in blood as a homodimeric protein consisting of two 94 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
MRGSHHHHHH GMASHMPSMS LCPMDEAISK KINQDFSSLL PAAMKNTVLH CWSVSSRGRL ASCPEGTTVT SCSCGSGCGS WDVREDTMCH CQCGSIDWTA ARCCTLRVGS.

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:

Trefoil Factor-3 Rat Recombinant

Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.

Product # :

CYT-781

Price :

Quantity :

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Shipped at Room temp

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Description

The Trefoil Factor-3 Rat was constructed as a recombinant protein with a 9 a.a C-terminal fusion of Flag-Tag (1 aa N-terminal+8 aa C-terminal). The TFF3 Rat produced in E.coli, is 7.7kDa protein containing a total of 68 amino acid residues.

Source

Escherichia Coli.

Formulation

TFF3 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM TRIS and 50mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.
Synonyms
Trefoil factor 3, Intestinal trefoil factor, rITF, Polypeptide P1.B, rP1.B, Tff3, Itf.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/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
MQEFVGLSPS QCMVPANVRV DCGYPTVTSE QCNNRGCCFD SSIPNVPWCF KPLQETECT F DYKDDDDK.

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:

Interferon-gamma Canine Recombinant

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-404

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Shipped at Room temp

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Description

Recombinant IFNG Dog produced in E.coli cells is a non-glycosylated, homodimeric protein containing 143 amino acid chain and having a molecular mass of 16.9kDa. IFNG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IFNG was lyophilized from a 0.2µm filtered concentrated solution in 25mM Sodium Succinate, pH 5.0, 60mM NaCl, with 0.1% 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 an anti-viral assay using A-72 canine fibroma cells infected with vesicular stomatitis virus (VSV) is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNG 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 IFNG in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QAMFFKEIEN LKEYFNASNP DVSDGGSLFV DILKKWREES DKTIIQSQIV SFYLKLFDNF KDNQIIQRSM DTIKEDMLGK FLNSSTSKRE DFLKLIQIPV NDLQVQRKAI NELIKVMNDL SPRSNLRKRK RSQNLFRGRR ASK
Background
What is the molecular weight/Mw of IFNG CANINE Protein?
IFNG CANINE Protein has a total Mw of 16.9kDa.

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

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

What is the Biological Activity of IFNG CANINE Protein?
The ED50 as determined by an anti-viral assay using A-72 canine fibroma cells infected with vesicular stomatitis virus (VSV) is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

What is the amino acid sequence of IFNG CANINE Protein?
QAMFFKEIEN LKEYFNASNP DVSDGGSLFV DILKKWREES DKTIIQSQIV SFYLKLFDNF KDNQIIQRSM DTIKEDMLGK FLNSSTSKRE DFLKLIQIPV NDLQVQRKAI NELIKVMNDL SPRSNLRKRK RSQNLFRGRR ASK

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

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

Complement Factor H Human

Complement factor H, H factor 1, CFH, HF, HF1, HF2.

Product # :

PRO-2700

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Description

Human Complement Factor H produced in Human plasma having a total molecular mass of 155kDa.

Source

Human Plasma.

Formulation

CFH protein solution contains PBS, pH 7.2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.
Synonyms
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
Physical Appearance
Sterile filtered solution.
Stability
CFH Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

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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