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Search results

1000 results found for “integrin”

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  • View Data Sheet

    Name :

    IMPAD1 Human, Active

    Description:

    Inositol Monophosphatase Domain Containing 1 Human Recombinant, BioActive

    Inositol monophosphatase 3, IMP 3, IMPase 3, EC 3.1.3.25, EC 3.1.3.7, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3, IMPAD1, IMPA3, GPAPP, IMP-3

    Product # :

    PRO-2638

    Price :

    Quantity :

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    • source
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    Description

    IMPAD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (34-359 a.a.) and having a molecular mass of 37.6kDa.IMPAD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IMPAD1 solution (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3300pmol/min/ug, and is defined as its ability to dephosphorylate adenosine 3'5'-diphosphate sodium slat at pH7.5, 25˚C.

    More Info

    • Introduction

      Inositol Monophosphatase Domain Containing 1 or IMPAD1 is a protein, part of the inositol monophosphatase group of proteins. The protein is found in Golgi apparatus and enhances phosphoadenosine phosphate hydrolysis to adenosine monophosphate. When Mutation in the IMPAD1 gene occurs leads to GRAPP type chondrodysplasia and therefore joint dislocations. On long arm chromosome 1 a pseudogene can be found.

    • Synonyms

      Inositol monophosphatase 3, IMP 3, IMPase 3, EC 3.1.3.25, EC 3.1.3.7, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3, IMPAD1, IMPA3, GPAPP, IMP-3

    • 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 MGSGRFSLFG LGGEPGGGAA GPAAAADGGT VDLREMLAVS VLAAVRGGDE VRRVRESNVL HEKSKGKTRE GAEDKMTSGD VLSNRKMFYL LKTAFPSVQI NTEEHVDAAD QEVILWDHKI PEDILKEVTT PKEVPAESVT VWIDPLDATQ EYTEDLRKYV TTMVCVAVNG KPMLGVIHKP FSEYTAWAMV DGGSNVKARS SYNEKTPRIV VSRSHSGMVK QVALQTFGNQ TTIIPAGGAG YKVLALLDVP DKSQEKADLY IHVTYIKKWD ICAGNAILKA LGGHMTTLSG EEISYTGSDG IEGGLLASIR MNHQALVRKL PDLEKTGHK

    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.

    Impad1 Protein
  • View Data Sheet

    Name :

    LGALS1 Human

    Description:

    Galectin-1 Human Recombinant

    Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.

    Product # :

    CYT-544

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    Quantity :

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    Shipped at Room temp

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    Description

    LGALS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids and having a molecular mass of 14.7kDa.The LGALS1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-1 protein was lyophilized from a concentrated (1mg/ml) containing 10mM sodium phosphate, pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x104 units/mg.

    More Info

    • Introduction

      The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 is an autocrine negative growth factor that regulates cell proliferation. Galectin-1 regulates cell apoptosis and cell differentiation. Galectin-1 binds CD45, CD3 and CD4 & inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of lyn kinase. Galectin-1 and its ligands are one of the master regulators of immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host–pathogen interactions. Galectin-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Galectin-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Galectin-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Galectin-1 expression is what should be developed for therapeutic applications against cancer progression. Galectin-1 is thus a promising molecular target for the development of new and original therapeutic tools. There is 88% homology between the human and mouse galectin-1.

    • Synonyms

      Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Galectin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-1 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 LGALS1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.

    • Background

      What is the molecular weight/Mw of LGALS1 HUMAN Protein?
      LGALS1 HUMAN Protein has a total Mw of 14.7kDa.

      What is the source or expression system of LGALS1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS1 HUMAN Protein?
      LGALS1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS1 HUMAN Protein?
      The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x104 units/mg.

      What is the amino acid sequence of LGALS1 HUMAN Protein?
      MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.

      What applications can LGALS1 HUMAN Protein be used in?
      LGALS1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS1 HUMAN Protein?
      The endotoxin level is minimal, LGALS1 HUMAN Protein was purified using conventional chromatography techniques.


    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.59 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).

    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.

    Galectin 1 Human
  • View Data Sheet

    Name :

    CD105 Human, Sf9

    Description:

    Endoglin Human Recombinant, Sf9

    CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    Product # :

    CYT-389

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

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

    Biological Activity

    Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

    More Info

    • Introduction

      Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
      The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

    • Synonyms

      CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

    • Background

      What is the molecular weight/Mw of CD105 Protein?
      CD105 Protein has a total Mw of 90kDa.

      What is the source or expression system of CD105 Protein?
      Sf9 Insect Cells.

      What is the Purity of CD105 Protein?
      CD105 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD105 Protein?
      Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

      What is the amino acid sequence of CD105 Protein?
      MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

      What applications can CD105 Protein be used in?
      CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD105 Protein?
      The endotoxin level is minimal, CD105 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.

    Endoglin Human Sf9
  • View Data Sheet

    Name :

    HBsAg adw

    Description:

    Hepatitis B Surface Antigen, adw Recombinant

    Product # :

    HBS-872

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    Description

    HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.

    Source

    Pichia Pastoris.

    Formulation

    Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

    • Physical Appearance

      Sterile Filtered pale solution.

    • Stability

      HBsAg Should be stored at 4°C.DO NOT FREEZE.

    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.

    Hbsag Adw
  • View Data Sheet

    Name :

    Activin-A Rat

    Description:

    Activin-A Rat Recombinant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-147

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    Description

    Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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

      Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 26.2 kDa.

      What is the source or expression system of Activin A Protein?
      Ecoli

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

      What is the Biological Activity of Activin A Protein?
      Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.

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

      What is the amino acid sequence of ACTIVIN A Protein?
      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

      What applications can ACTIVIN A 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.

    Inhba Rat
  • View Data Sheet

    Name :

    DCN Mouse

    Description:

    Decorin Mouse Recombinant

    Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.

    Product # :

    PRO-2234

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    Description

    DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.

    • Synonyms

      Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.

    • 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

      GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH

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    Dcn Mouse
  • View Data Sheet

    Name :

    IFNAR1 Mouse

    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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    • SDS-PAGE

    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

    IFNAR1 Mouse - Product image 1

    More Info

    • 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.

    Ifnar1 Mouse
  • View Data Sheet

    Name :

    SPINK7 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant

    Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    Product # :

    PRO-1507

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    Description

    SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma

    • Synonyms

      Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    • 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 MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.

    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.

    Spink7 Human
  • View Data Sheet

    Name :

    STX17 Human

    Description:

    Syntaxin-17 Human Recombinant

    Syntaxin 17

    Product # :

    PRO-1712

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    Description

    STX17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229) and having a molecular mass of 28.6kDa.STX17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STX17 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STX17 is a member of to the syntaxin family and contains 1 t-SNARE coiled-coil homology domain. STX17 is involved in vesicle trafficking to lysosomes and takes part in procedures associated with cell division.

    • Synonyms

      Syntaxin 17

    • 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 MGSMSEDEEK VKLRRLEPAI QKFIKIVIPT DLERLRKHQI NIEKYQRCRI WDKLHEEHIN AGRTVQQLRS NIREIEKLCL KVRKDDLVLL KRMIDPVKEE ASAATAEFLQ LHLESVEELK KQFNDEETLL QPPLTRSMTV GGAFHTTEAE ASSQSLTQIY ALPEIPQDQN AAESWETLEA DLIELSQLVT DFSLLVNSQQ EKIDSIADHV NSAAVNVEEG TKNLGKAAKY KL

    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.

    Stx17 Human
  • View Data Sheet

    Name :

    CRYGS Human

    Description:

    Crystallin, Gamma S Human Recombinant

    Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.

    Product # :

    PRO-963

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    Description

    CRYGS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178) and having a molecular mass of 23.6 kDa.The CRYGS is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mammalian crystallins which are water soluble structural proteins located in the vertebrate eye are classified in three forms, labeled alpha, beta and gamma. Crystallins, the primary components of the lens, raise the refractive index of the eye all through the accommodation by creating high-molecular weight aggregates that maintain transparency. CRYGS is a monomer that does not aggregate. CRYGS encodes the most substantial gamma-crystallin in adult eye lens tissue. Gamma-crystallins has a part in cataract formation due to aging or mutations in specific genes,

    • Synonyms

      Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.

    • 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 MGSHMSKTGT KITFYEDKNF QGRRYDCDCD CADFHTYLSR CNSIKVEGGT WAVYERPNFA GYMYILPQGE YPEYQRWMGL NDRLSSCRAV HLPSGGQYKI QIFEKGDFSG QMYETTEDCP SIMEQFHMRE IHSCKVLEGV WIFYELPNYR GRQYLLDKKE YRKPIDWGAA SPAVQSFRRI VE

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    Crygs Human
  • View Data Sheet

    Name :

    NCALD Human

    Description:

    Neurocalcin Delta Recombinant Human

    Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    Product # :

    PRO-093

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    Description

    NCALD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-193.a.a) and having a molecular mass of 24.4kDa. NCALD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NCALD protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCALD belongs to the neuronal calcium sensor (NCS) family. NCALD is cytosolic at inactive calcium levels; but, high intracellular calcium levels induce a conformational transformation which exposes the myristoyl group, causing protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is a regulator of signal transduction by G protein-coupled receptor.

    • Synonyms

      Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA GQF.

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    Ncald Human
  • View Data Sheet

    Name :

    ATPIF1 Human

    Description:

    ATPase Inhibitory Factor 1 Human Recombinant

    ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.

    Product # :

    PRO-1154

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    Description

    ATPIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (26-106 a.a) and having a molecular mass of 12.2kDa.ATPIF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ATPIF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATPase inhibitory factor 1 (ATPIF1) attaches to the C-terminal region of a beta subunit of the F1-ATPase at low pH values and, through interference of the beta and gamma subunit interaction, ATPIF1 controls the activity of the F1 (the hydrophilic catalytic core), F0 (the membrane embedded protein channel) ATPase. ATPIF1 overexpression in a number of human carcinomas additionally reinforces its participation in oncogenesis and offers insight into the transformed metabolism of cancer cells, including the reprogramming of energy metabolism in relation to glycolysis. Endogenous F1F(o)-ATPase inhibitor curbing ATP depletion when the mitochondrial membrane potential drops below a threshold and the F1F(o)-ATP synthase begins hydrolyzing ATP to pump protons out of the mitochondrial matrix.

    • Synonyms

      ATPase inhibitor mitochondrial, Inhibitor of F(1)F(o)-ATPase, IF(1), IF1, ATPIF1, ATPI, IP, ATPIP.

    • 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 MGSHMGSDQS ENVDRGAGSI REAGGAFGKR EQAEEERYFR AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK MLKHDD.

    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.

    Atpif1 Human
  • View Data Sheet

    Name :

    PTX3 Human

    Description:

    Pentraxin-3 Human Recombinant

    TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    Product # :

    PRO-694

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    Description

    Recombinant Human PTX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (18-381 a.a) and having a molecular mass of 44.4 kDa. PTX3 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTX3 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.

    • Synonyms

      TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS DDYDLMYVNL DNEIDNGLHP TEDPTPCDCG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S.

    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.

    Ptx3 Human
  • View Data Sheet

    Name :

    SGTA Antibody

    Description:

    Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha, Mouse Anti Human

    alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.

    Product # :

    ANT-631

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    Formulation

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

    More Info

    • Introduction

      SGTA is a ubiquitously expressed protein that contains three TPR protein-protein interaction duplicates. SGTA takes part as a component of the androgen receptor (AR)-chaperone-cochaperone complex, functions as a cochaperone and participates in androgen signaling. SGTA binds directly to HSC70 and HSP70 and mediates their ATPase activity. SGTA gene encodes a protein that is able to interact with the chief nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate. In addition, SGTA interacts with Vpu and Gag from HIV-1, SARS-CoV accessory protein 7a, DNAJC5 and DNAJC5B. Since this transcript is expressed universally in several tissues, SGTA serves a housekeeping function. While being involved in apoptosis and androgen signaling, SGTA is a possible molecule for polycystic ovary syndrome, a disorder characterized by androgen excess, obesity and menstrual disturbances.

    • Synonyms

      alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human SGTA mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human SGTA protein 1-313 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT19E8AT.

    • Applications

      The 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

      SGTA 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.

    Sgta Antibody
  • View Data Sheet

    Name :

    FGF 2 Human (147 a.a.)

    Description:

    Fibroblast Growth Factor Basic 147 a.a. Human Recombinant

    Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

    Product # :

    CYT-557

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    Description

    Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16.5kDa. The FGF2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The bFGF was lyophilized from a sterile filtered solution containing 20mM Tris-HCl, pH 7.6 and 150mM NaCl.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.

    More Info

    • Introduction

      FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized basic-FGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFb should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF-B in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

    • Background

      What is the molecular weight/Mw of FGF 2 Protein?
      FGF 2 Protein has a total Mw of 16.5kDa.

      What is the source or expression system of FGF 2 Protein?
      Escherichia Coli.

      What is the Purity of FGF 2 Protein?
      FGF 2 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 2 Protein?
      The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.

      What is the amino acid sequence of FGF 2 Protein?
      MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

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

      What is the endotoxin level for FGF 2 Protein?
      The endotoxin level is minimal, FGF 2 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.

    Fgf 2 147 Aa Human
  • View Data Sheet

    Name :

    AREG Human

    Description:

    Amphiregulin Human Recombinant

    Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

    Product # :

    CYT-041

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    Description

    Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa.The AREG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

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

    Biological Activity

    Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

    More Info

    • Synonyms

      Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized AREG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AREG 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 AREG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

    • Background

      Amphiregulin Human Recombinant: Exploring its Role in Cancer Biology and Therapeutic Applications

      Abstract:


      Amphiregulin, a member of the epidermal growth factor (EGF) family, has gained significant attention in cancer research. This research paper provides an overview of Amphiregulin human recombinant, highlighting its molecular characteristics, signaling pathways, and therapeutic potential. Understanding the multifaceted role of Amphiregulin opens avenues for targeted cancer therapies. This article provides a concise analysis of Amphiregulin, emphasizing its impact on cancer biology and its therapeutic applications.

      Introduction:


      Cancer continues to be a significant health challenge worldwide, necessitating novel therapeutic approaches. Amphiregulin, an EGF family member, has emerged as a promising target in cancer research. This paper provides an overview of Amphiregulin, shedding light on its structure, function, and therapeutic potential.

      Amphiregulin Signaling and Mechanisms:


      Amphiregulin exerts its effects through the binding and activation of the EGF receptor (EGFR). Upon activation, a cascade of intracellular signaling pathways is triggered, including the MAPK and PI3K/AKT pathways. These pathways regulate critical cellular processes such as cell proliferation, survival, migration, and angiogenesis.

      Amphiregulin in Cancer Biology:


      Amphiregulin has been implicated in various aspects of cancer biology, including tumor growth, metastasis, and resistance to therapy. Its overexpression is observed in several cancer types, and its role in promoting tumor growth and metastasis has been demonstrated in preclinical studies. Targeting Amphiregulin signaling shows promise in inhibiting cancer progression and overcoming therapy resistance.

      Therapeutic Potential of Amphiregulin Human Recombinant:


      Amphiregulin human recombinant holds significant therapeutic potential in cancer treatment. Strategies aimed at blocking Amphiregulin-EGFR interactions or inhibiting downstream signaling pathways are being explored as potential therapeutic interventions. Additionally, Amphiregulin could serve as a predictive biomarker to identify patients who are more likely to respond to targeted therapies.

      Challenges and Future Directions:


      While the therapeutic targeting of Amphiregulin shows promise, several challenges need to be addressed. Further research is required to fully understand the complex interplay between Amphiregulin and other molecular pathways in cancer biology. Additionally, the development of specific and potent inhibitors and the identification of patient selection criteria are important considerations for successful clinical translation.

      Conclusion:


      Amphiregulin human recombinant represents a promising avenue for targeted cancer therapy. Understanding the molecular mechanisms and functional implications of Amphiregulin in cancer biology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve patient outcomes and contribute to the advancement of personalized medicine.

      What is the molecular weight/Mw of AREG Protein?
      AREG Protein has a total Mw of 11.3kDa.

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

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

      What is the Biological Activity of AREG Protein?
      Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

      What is the amino acid sequence of AREG Protein?
      SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

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

      What is the endotoxin level for AREG Protein?
      The endotoxin level is minimal, AREG 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.

    Areg Human
  • View Data Sheet

    Name :

    B.Microti IRA

    Description:

    Babesia Microti IRA Recombinant

    Product # :

    PRO-2268

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    Description

    Recombinant Babesia Microti IRA produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 77,554 Dalton. B.Microti IRA is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    B.Microti IRA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Babesiosis is a disease caused by apicomplexan parasites of the Babesia genus. The Babesia microti life cycle involves 2 hosts, which include a rodent, mainly the white-footed mouse (Peromyscus leucopus) and a tick in the Ixodes genus. During a blood meal, a Babesia-infected tick introduces sporozoites into the mouse host. Sporozoites pass into the erythrocytes and undergo asexual reproduction (budding). In the blood, some parasites differentiate into male and female gametes, though these cannot be distinguished by light microscopy. The definitive host is the tick. Once ingested by an proper tick, gametes unite and undergo a sporogonic cycle resulting in sporozoites. Transovarial transmission (aka vertical or hereditary transmission) has been detected for "large" Babesia species but not for the "small" Babesia, such as B. microti. Humans enter the cycle when bitten by the infected ticks. Thus during a blood meal, a Babesia-infected tick introduces sporozoites into the human host. Sporozoites then enter erythrocytes and undergo asexual replication (budding). Multiplication of the blood-stage parasites is responsible for the clinical manifestations of the disease. Humans typically are dead-end hosts. However, human-to-human transmission is well acknowledged to occur via contaminated blood transfusions.

    • 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.

    Bmicroti Ira
  • View Data Sheet

    Name :

    sRANKL Human

    Description:

    RANK Ligand Soluble Human Recombinant

    Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    Product # :

    CYT-334

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    • HPLC, SDS-PAGE

    Description

    sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.7kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Sodium phosphate, pH-7.5.

    Purity

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

    Biological Activity

    The activity of RAW-Blue was measured to be 46.96 ng/ml, corresponding to a specific activity of 2.1x104 units/mg.

    HPLC, SDS-PAGE

    sRANKL Human HPLC - Product image 1
    sRANKL Human SDS PAGE - Product image 2

    More Info

    • Introduction

      RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

    • Synonyms

      Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized sRANKL in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKAMVDGSW LDLAKRSKLE AQPFAHLTIN ATDIPSGSHK VSLSSWYHDR GWAKISNMTF SNGKLIVNQD GFYYLYANIC FRHHETSGDL ATEYLQLMVY VTKTSIKIPS SHTLMKGGST KYWSGNSEFH FYSINVGGFF KLRSGEEISI EVSNPSLLDP DQDATYFGAF KVRDID.

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    Rankl Human
  • View Data Sheet

    Name :

    GKN3P Human

    Description:

    Gastrokine 3 Human Recombinant

    Gastrokine 3 Pseudogene, Gastrokine-3, GKN3P.

    Product # :

    PRO-2033

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    Description

    GKN3P Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met21-Leu181) containing 171 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 19.4kDa.

    Source

    Escherichia Coli.

    Formulation

    GKN3P filtered (0.4µm) solution at a concentration of 0.3mg/ml in 0.03M acetate buffer, pH 4.0 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gastrokine 3 (GKN3P) is a Pseudogene, which May inhibit gastric epithelial cell proliferation.

    • Synonyms

      Gastrokine 3 Pseudogene, Gastrokine-3, GKN3P.

    • Physical Appearance

      Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MKHHHHHHASMMNIRFNHPL YGSFGTQIIH IGAFQGMVSI RDNNIFSEWD GILDYKNALL VAKVFNKMAC VLARMDKAVF PSLDDISKAL DKQAFKYYPS TRGLTYTVLP SWVKNLAQYG KPIKNMCRDD PTYFAQQQKE GTALAIDSNS CFEIQLLSFM GLFICGETPG L.

    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.

    Gkn3P Human
  • View Data Sheet

    Name :

    CD44 Human

    Description:

    CD44 Human Recombinant

    CD44 Molecule (Indian Blood Group), Hematopoietic Cell E- And L-Selectin Ligand, GP90 Lymphocyte Homing/Adhesion Receptor, Chondroitin Sulfate Proteoglycan 8, Extracellular Matrix Receptor III, Heparan Sulfate Proteoglycan, Phagocytic Glycoprotein 1, Hyaluronate Receptor, Hermes Antigen, ECMR-III, HUTCH-I, Epican, CDW44, MDU2, MDU3, MIC4, LHR, CD44 Antigen (Homing Function And Indian Blood Group System),Homing Function And Indian Blood Group System, Cell Surface Glycoprotein CD44, Phagocytic Glycoprotein I, Soluble CD44, CSPG8, HCELL, PGP-1, PGP-I, MC56, Pgp1, IN, CD44 .

    Product # :

    PRO-2540

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    Description

    CD44 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (21-220 a.a.) and fused to a 239 aa hIgG-His-tag at C-terminus containing a total of 439 amino acids and having a molecular mass of 49kDa.CD44 shows multiple bands between 57-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD44 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD44 is a cell-surface glycoprotein that plays a role in cell-cell interactions, cell adhesion and migration. CD44 is a receptor for hyaluronic acid and also interacts with other ligands, such as osteopontin, collagens, and matrix metalloproteinases. CD44 participates in a wide variety of cellular functions such as lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis.

    • Synonyms

      CD44 Molecule (Indian Blood Group), Hematopoietic Cell E- And L-Selectin Ligand, GP90 Lymphocyte Homing/Adhesion Receptor, Chondroitin Sulfate Proteoglycan 8, Extracellular Matrix Receptor III, Heparan Sulfate Proteoglycan, Phagocytic Glycoprotein 1, Hyaluronate Receptor, Hermes Antigen, ECMR-III, HUTCH-I, Epican, CDW44, MDU2, MDU3, MIC4, LHR, CD44 Antigen (Homing Function And Indian Blood Group System),Homing Function And Indian Blood Group System, Cell Surface Glycoprotein CD44, Phagocytic Glycoprotein I, Soluble CD44, CSPG8, HCELL, PGP-1, PGP-I, MC56, Pgp1, IN, CD44 .

    • 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

      QIDLNITCRF AGVFHVEKNG RYSISRTEAA DLCKAFNSTL PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN ASAPPEEDCT SVTDLPNAFD GPITITIVNR DGTRYVQKGE YRTNPEDIYP SNPTDDDVSS GSSSERSSTS GGYIFYTFST VHPIPDEDSP WITDSTDRIP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

    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.

    Cd44 Human
  • View Data Sheet

    Name :

    CFD Human

    Description:

    Complement Factor D Human

    Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.

    Product # :

    PRO-2699

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    Description

    Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.

    Source

    Human Plasma.

    Formulation

    CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.

    • Synonyms

      Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFD 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.

    Cfd Human
  • View Data Sheet

    Name :

    IGF1 PAT6F8AT Antibody

    Description:

    Insulin-Like Growth Factor-1 Clone PAT6F8AT, Mouse Anti Human

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    Product # :

    ANT-538

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    • formulation
    • More Info

    Formulation

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

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    • Introduction

      The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human IGF1 mAb, clone PAT6F8AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IGF1 protein 49-118 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT6F8AT.

    • Applications

      HSPA5 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      IGF1 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.

    Igf1 Pat6F8At Antibody
  • View Data Sheet

    Name :

    MIF Antibody

    Description:

    Macrophage Migration Inhibitory Factor, Mouse Anti Human

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

    Product # :

    ANT-311

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    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

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

    • Immunogen

      Anti-human MIF mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human MIF amino acids 1-114 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P4E4AT.

    • Applications

      MIF 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

      MIF antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Mif Antibody
  • View Data Sheet

    Name :

    ACTA2 Human

    Description:

    Actin, Alpha 2, Smooth Muscle, Aorta Human Recombinant

    Actin Alpha 2 Smooth Muscle Aorta, Cell Growth-Inhibiting Gene 46 Protein, Actin Aortic Smooth Muscle, Alpha-Cardiac Actin, Alpha-Actin-2, MYMY5, ACTSA, ACTVS, AAT6.

    Product # :

    PRO-1220

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    • source
    • formulation
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    • More Info

    Description

    ACTA2 Human Recombinant produced in E. coli is a single polypeptide chain containing 400 amino acids (3-377) and having a molecular mass of 44.4 kDa.ACTA2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ACTA2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACTA2 is a member of the actin family of proteins, an extremely conserved family of proteins which takes part in cell motility, structure and integrity. Three types of actin isoforms are known: Alpha, beta and gamma. Alpha actins are a main factor of the contractile mechanism, and beta and gamma take part in the regulation of cell motility. ACTA2 is an alpha actin which is located in skeletal muscle. Mutations in ACTA2 cause aortic aneurysm familial thoracic type 6. Various alternatively spliced variants, encoding the same protein were identified.

    • Synonyms

      Actin Alpha 2 Smooth Muscle Aorta, Cell Growth-Inhibiting Gene 46 Protein, Actin Aortic Smooth Muscle, Alpha-Cardiac Actin, Alpha-Actin-2, MYMY5, ACTSA, ACTVS, AAT6.

    • 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 MGSHMEEEDS TALVCDNGSG LCKAGFAGDD APRAVFPSIV GRPRHQGVMV GMGQKDSYVG DEAQSKRGIL TLKYPIEHGI ITNWDDMEKI WHHSFYNELR VAPEEHPTLL TEAPLNPKAN REKMTQIMFE TFNVPAMYVA IQAVLSLYAS GRTTGIVLDS GDGVTHNVPI YEGYALPHAI MRLDLAGRDL TDYLMKILTE RGYSFVTTAE REIVRDIKEK LCYVALDFEN EMATAASSSS LEKSYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVLSGGTTM YPGIADRMQK EITALAPSTM KIKIIAPPER KYSVWIGGSI LASLSTFQQM WISKQEYDEA GPSIVHRKCF.

    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.

    Acta2 Human
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