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Search results

652 results found for “biglycan”

Name

Description

Product #

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  • View Data Sheet

    Name :

    BGN Mouse

    Description:

    Biglycan Mouse Recombinant

    BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    Product # :

    PRO-2537

    Price :

    Quantity :

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    • source
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    • More Info

    Description

    BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 574 amino acids (38-369 a.a.) and having a molecular mass of 64.6kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). BGN is expressed with a 242 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    The BGN solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

    • Synonyms

      BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    • 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

      ADPDEEASGS DTTSGVPDLD SVTPTFSAMC PFGCHCHLRV VQCSDLGLKT VPKEISPDTT LLDLQNNDIS ELRKDDFKGL QHLYALVLVN NKISKIHEKA FSPLRKLQKL YISKNHLVEI PPNLPSSLVE LRIHDNRIRK VPKGVFSGLR NMNCIEMGGN PLENSGFEPG AFDGLKLNYL
      RISEAKLTGI PKDLPETLNE LHLDHNKIQA IELEDLLRYS KLYRLGLGHN QIRMIENGSL SFLPTLRELH LDNNKLSRVP AGLPDLKLLQ VVYLHSNNIT KVGINDFCPM GFGVKRAYYN GISLFNNPVP YWEVQPATFR CVTDRLAIQF GNYKKLEPKS CDKTHTCPPC PAPELLGGPS
      VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH 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.

    Biglycan Mouse
  • View Data Sheet

    Name :

    BGN Human

    Description:

    Biglycan Human Recombinant

    DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.

    Product # :

    PRO-1382

    Price :

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    • More Info

    Description

    BGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (38-368a.a) and having a molecular mass of 39.5kDa. BGN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

    • Synonyms

      DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.

    • 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 MDEEASGADT SGVLDPDSVT PTYSAMCPFG CHCHLRVVQC SDLGLKSVPK EISPDTTLLD LQNNDISELR KDDFKGLQHL YALVLVNNKI SKIHEKAFSP LRKLQKLYIS KNHLVEIPPN LPSSLVELRI HDNRIRKVPK GVFSGLRNMN CIEMGGNPLE NSGFEPGAFD GLKLNYLRIS EAKLTGIPKD LPETLNELHL DHNKIQAIEL EDLLRYSKLY RLGLGHNQIR MIENGSLSFL PTLRELHLDN NKLARVPSGL PDLKLLQVVY LHSNNITKVG VNDFCPMGFG VKRAYYNGIS LFNNPVPYWE VQPATFRCVT DRLAIQFGNY KK.

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

    Bgn Human
  • View Data Sheet

    Name :

    BGN Human, Sf9

    Description:

    Biglycan Human Recombinant, Sf9

    BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    Product # :

    PRO-2536

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 340 amino acids (38-368 a.a.) and having a molecular mass of 38.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). BGN is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    The BGN solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is ≤ 20 ug/ml. The specific activity is measured by inhibiting the cell growth using 3T3‑ L1 mouse embryonic  fibroblast  adipose-like cells.

    More Info

    • Introduction

      Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.

    • Synonyms

      BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.

    • 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

      ADPDEEASGA DTSGVLDPDS VTPTYSAMCP FGCHCHLRVV QCSDLGLKSV PKEISPDTTL LDLQNNDISE LRKDDFKGLQ HLYALVLVNN KISKIHEKAF SPLRKLQKLY ISKNHLVEIP PNLPSSLVEL RIHDNRIRKV PKGVFSGLRN MNCIEMGGNP LENSGFEPGA FDGLKLNYLR ISEAKLTGIP KDLPETLNEL HLDHNKIQAI ELEDLLRYSK LYRLGLGHNQ IRMIENGSLS FLPTLRELHL DNNKLARVPS GLPDLKLLQV VYLHSNNITK VGVNDFCPMG FGVKRAYYNG ISLFNNPVPY WEVQPATFRC VTDRLAIQFG NYKKHHHHHH.

    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.

    Biglycan Human
  • View Data Sheet

    Name :

    LUM Human, sf9

    Description:

    Lumican Human Recombinant, Sf9

    Lumican, LDC, Lumican Proteoglycan, Keratan Sulfate Proteoglycan Lumican, SLRR2D, KSPG Lumican.

    Product # :

    PRO-2355

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    LUM Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 329 amino acids (19-338 aa) and having a molecular mass of 37.7kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).LUM is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lumican also known as LUM belongs to the small leucine-rich proteoglycan (SLRP) family which comprises decorin, biglycan, fibromodulin, keratocan, epiphycan, and osteoglycin. Furthermore we can see that in these bifunctional molecules, the protein moiety binds collagen fibrils and the highly charged hydrophilic glycosaminoglycans regulate interfibrillar spacings. Lumican is the main keratan sulfate proteoglycan of the cornea however LUM is also distributed in interstitial collagenous matrices throughout the body. Lumican regulates collagen fibril organization and circumferential growth, corneal transparency, epithelial cell migration and tissue repair. Among the diseases associated with LUM is posterior amorphous corneal dystrophy.

    • Synonyms

      Lumican, LDC, Lumican Proteoglycan, Keratan Sulfate Proteoglycan Lumican, SLRR2D, KSPG Lumican.

    • 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

      ADLQYYDYDF PLSIYGQSSP NCAPECNCPE SYPSAMYCDE LKLKSVPMVP PGIKYLYLRN NQIDHIDEKA FENVTDLQWL ILDHNLLENS KIKGRVFSKL KQLKKLHINH NNLTESVGPL PKSLEDLQLT HNKITKLGSF EGLVNLTFIH LQHNRLKEDA VSAAFKGLKS LEYLDLSFNQ IARLPSGLPV SLLTLYLDNN KISNIPDEYF KRFNALQYLR LSHNELADSG IPGNSFNVSS LVELDLSYNK LKNIPTVNEN LENYYLEVNQ LEKFDIKSFC KILGPLSYSK IKHLRLDGNR ISETSLPPDM YECLRVANEV TLNHHHHHH

    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.

    Lum Human Sf9
  • View Data Sheet

    Name :

    LUM Human

    Description:

    Lumican Human Recombinant

    Lumican, LDC, Lumican Proteoglycan, Keratan Sulfate Proteoglycan Lumican, SLRR2D, KSPG Lumican.

    Product # :

    PRO-1821

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    Description

    LUM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (19-338a.a) and having a molecular mass of 39kDa. LUM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LUM protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lumican also known as LUM belongs to the small leucine-rich proteoglycan (SLRP) family which comprises decorin, biglycan, fibromodulin, keratocan, epiphycan, and osteoglycin. Furthermore we can see that in these bifunctional molecules, the protein moiety binds collagen fibrils and the highly charged hydrophilic glycosaminoglycans regulate interfibrillar spacings. Lumican is the main keratan sulfate proteoglycan of the cornea however LUM is also distributed in interstitial collagenous matrices throughout the body. Lumican regulates collagen fibril organization and circumferential growth, corneal transparency, epithelial cell migration and tissue repair. Among the diseases associated with LUM is posterior amorphous corneal dystrophy.

    • Synonyms

      Lumican, LDC, Lumican Proteoglycan, Keratan Sulfate Proteoglycan Lumican, SLRR2D, KSPG Lumican.

    • 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 MGSQYYDYDF PLSIYGQSSP NCAPECNCPE SYPSAMYCDE LKLKSVPMVP PGIKYLYLRN NQIDHIDEKA FENVTDLQWL ILDHNLLENS KIKGRVFSKL KQLKKLHINH NNLTESVGPL PKSLEDLQLT HNKITKLGSF EGLVNLTFIH LQHNRLKEDA VSAAFKGLKS LEYLDLSFNQ IARLPSGLPV SLLTLYLDNN KISNIPDEYF KRFNALQYLR LSHNELADSG IPGNSFNVSS LVELDLSYNK LKNIPTVNEN LENYYLEVNQ LEKFDIKSFC KILGPLSYSK IKHLRLDGNR ISETSLPPDM YECLRVANEV TLN.

    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.

    Lum Human
  • View Data Sheet

    Name :

    SDC4 Human

    Description:

    Syndecan-4 Human Recombinant

    SDC-4, SYND4, SYND-4, Amphiglycan, Ryudocan core protein, Syndecan-4.

    Product # :

    PRO-778

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    Description

    SDC4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids (19-145a.a.) and having a molecular mass of 13.9 kDa. SDC4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Syndecan-4 (1mg/ml) protein solution containing 20mM Tris-HCl pH-8, and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Syndecan-4 is a type I integral membrane heparan sulfate proteoglycan (HSPG), which was originally isolated from cloned rat microvascular endothelial cells as an antithrombin-binding molecule, and is now known to be a member of the syndecan family. Syndecan-4 binds to basic fibroblast growth factor (bFGF), midkine, and tissue factor pathway inhibitor via its heparan sulfate chains, and is thought to be involved in various biologic functions such as signaling of bFGF, anticoagulation, and focal adhesion formation. A previous study demonstrated that syndecan-4 is expressed in various tissues, and its level of expression in the kidney is stronger than those of other syndecan family members. Thus, syndecan-4 is thought to play certain roles in maintaining renal function. Moreover, it has been reported that proteoglycans, especially sulfated proteoglycans, are involved in organogenesis of the kidney.

    • Synonyms

      SDC-4, SYND4, SYND-4, Amphiglycan, Ryudocan core protein, Syndecan-4.

    • 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). Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MESIRETEVI DPQDLLEGRY FSGALPDDED VVGPGQESDD FELSGSGDLD DLEDSMIGPE VVHPLVPLDN HIPERAGSGS QVPTEPKKLE ENEVIPKRIS PVEESEDVSN KVSMSSTVQG SNIFERTE.

    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.

    Sdc4 Human
  • View Data Sheet

    Name :

    BMP 4 Human

    Description:

    Bone Morphogenetic Protein-4 Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-361

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    Description

    Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

    Purity

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

    More Info

    • Introduction

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant

      As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.

      Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.

      Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!

      How Does Bone Morphogenetic Protein-4 (BMP-4) Work?

      Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.

      The Role of BMP-4

      This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.

      However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:

      • Embryonic development
      • Wound healing
      • Bone remodeling
      • Immune response modulation
      • Tissue repair
      • Cardiac development and function

      What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?

      To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.

      As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.

      More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:

      • Cancer therapy
      • Development of engineered tissues and organs
      • Bone regeneration for the treatment of osteoporosis and nonunion fractures
      • Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
      • Promotion of tissue repair and regeneration

      Final Thoughts BMP-4

      Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.

      However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP4 Protein?
      Escherichia Coli.

      What is the Purity of BMP4 Protein?
      BMP4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP4 Protein?
      The biological functionality of BMP4 Protein will be determined in the future.

      What is the amino acid sequence of BMP4 Protein?
      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

      What applications can BMP4 Protein be used in?
      BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 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.

    Bmp4 Human
  • View Data Sheet

    Name :

    Glycinin

    Description:

    Allergen Ara h 3.0101 Recombinant

    Glycinin, Arah3.

    Product # :

    ALR-008

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    Description

    Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.

    • Synonyms

      Glycinin, Arah3.

    • 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.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Glycinin
  • View Data Sheet

    Name :

    Glucagon Human

    Description:

    Glucagon Human Recombinant

    GLP1, GLP2, GRPP.

    Product # :

    HOR-237

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    Description

    Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton. The Glucagon is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of recombinant Glucagon was formulated with 100mg of lactose.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.

    More Info

    • Introduction

      Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
      Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.

    • Synonyms

      GLP1, GLP2, GRPP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Glucagon although stable at room temperature for 3 weeks, should be stored at 40C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.

    • Background

      What is the molecular weight/Mw of GLUCAGON HUMAN Protein?
      GLUCAGON HUMAN Protein has a total Mw of 3.48kDa.

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

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

      What is the Biological Activity of GLUCAGON HUMAN Protein?
      The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.

      What is the amino acid sequence of GLUCAGON HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.

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

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

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

    Glucagon Human Recombinant
  • View Data Sheet

    Name :

    IFIH1 Human

    Description:

    Interferon Induced With Helicase C Domain 1 Human Recombinant

    Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    Product # :

    PRO-1505

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    Description

    IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

    • Synonyms

      Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    • 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.

    Ifih1 Human
  • View Data Sheet

    Name :

    SDC1 Human

    Description:

    Syndecan-1 Human Recombinant

    Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.

    Product # :

    PRO-1065

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    Description

    SDC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 262 amino acids (18-254) and having a molecular mass of 27kDa (molecular size on SDS-PAGE will appear higher).SDC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SDC1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      CD138 takes a part in cell adhesion. CD138 is expressed on the surface of pre-B cells and plasma cells but is absent from mature B cells. SDC1 is a selective marker for B cell lymphoblastic leukemia and lymphoplasmacytoid leukemia. SDC1 is missing from the apoptotic myeloma cells; therefore is a valuable marker for plasma cell and myeloma cells.

    • Synonyms

      Heparan Sulfate proteoglycan fibroblast growth factor receptor, syndecan proteoglycan 1, Syndecan 1, SYND1, CD138 antigen, SDC.

    • 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 MGSHMQPALP QIVATNLPPE DQDGSGDDSD NFSGSGAGAL QDITLSQQTP STWKDTQLLT AIPTSPEPTG LEATAASTST LPAGEGPKEG EAVVLPEVEP GLTAREQEAT PRPRETTQLP TTHQASTTTA TTAQEPATSH PHRDMQPGHH ETSTPAGPSQ ADLHTPHTED GGPSATERAA EDGASSQLPA AEGSGEQDFT FETSGENTAV VAVEPDRRNQ SPVDQGATGA SQGLLDRKEV LG.

    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.

    Sdc1 Human
  • View Data Sheet

    Name :

    RCAN2 Human

    Description:

    Regulator of Calcineurin 2 Human Recombinant

    Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).

    Product # :

    PRO-990

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    Description

    RCAN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-197 a.a.) and having a molecular mass of 24.1kDa.RCAN2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RCAN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      RCAN2 is a member of the RCAN (Regulator of calcineurin) family that controls the activity of Calcineurin using a valine-rich region placed in their carboxyl tail. RCANs race against NFAT (nuclear factor of activated T-cells) to bind to the same docking site in calcineurin, and consequently inhibits or activates calcineurin activity. RCAN2 is a Ca(2+) dependent protein phosphatase which takes part in numerous neuornal functions.

    • Synonyms

      Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).

    • 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 MPAPSMDCDV STLVACVVDV EVFTNQEVKE KFEGLFRTYD DCVTFQLFKS FRRVRINFSN PKSAARARIE LHETQFRGKK LKLYFAQVQT PETDGDKLHL APPQPAKQFL ISPPSSPPVG WQPINDATPV LNYDLLYAVA KLGPGEKYEL HAGTESTPSV VVHVCDSDIE EEEDPKTSPK PKIIQTRRPG LPPSVSN

    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.

    Rcan2 Human
  • View Data Sheet

    Name :

    RCAN1 Human

    Description:

    Regulator of Calcineurin 1 Human Recombinant

    Calcipressin-1, Regulator of calcineurin 1, Down syndrome critical region protein 1, Myocyte-enriched calcineurin-interacting protein 1, MCIP1, Adapt78, RCAN1, ADAPT78, CSP1, DSC1, DSCR1, RCN1.

    Product # :

    PRO-319

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    Description

    RCAN1 Isoform-b Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids and having a molecular mass of 13 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-7.5, 100mM NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RCAN1 encoded by a gene located in the human chromosome 21, interacts with calcineurin A and inhibits calcineurin-dependent signaling pathways, possibly affecting central nervous system development. RCAN1 is located in the minimal candidate region for the Down syndrome phenotype, and is over expressed in the brain of Down syndrome fetuses. Chronic over expression of this gene may lead to neurofibrillary tangles such as those associated with Alzheimer disease. Three transcript variants encoding three different isoforms have been found for this gene.
      DSCR1 Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A, possibly affecting central nervous system development.

    • Synonyms

      Calcipressin-1, Regulator of calcineurin 1, Down syndrome critical region protein 1, Myocyte-enriched calcineurin-interacting protein 1, MCIP1, Adapt78, RCAN1, ADAPT78, CSP1, DSC1, DSCR1, RCN1.

    • 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

      MKLYFAQTLH IGSSHLAPPN PDKQFLISPP ASPPVGWKQV EDATPVINYD LLYAISKLGPGEKYELHAAT DTTPSVVVHV CESDQEKEEE EEMERMRRPK PKIIQTRRPE YTPIHLS.

    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.

    Rcan1 Human
  • View Data Sheet

    Name :

    HAPLN1 Human

    Description:

    Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant

    Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    Product # :

    PRO-2012

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    Description

    HAPLN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (16-354 a.a.) and having a molecular mass of 40.9kDa.HAPLN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAPLN1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hyaluronan And Proteoglycan Link Protein 1, which is also known as HAPLN1 is a part of the HAPLN family.HAPLN1 contains one Ig-like V-type domain and two Link domains. In the extracellular cartilage matrix, HAPLN1 stabilizes the aggregates of proteoglycan monomers by means of hyaluronic acid .

    • Synonyms

      Hyaluronan and proteoglycan link protein 1 precursor, CRTL1, Cartilage-linking protein 1, Cartilage-link protein, Proteoglycan link protein, HAPLN1.

    • 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 MGSDHLSDNY TLDHDRAIHI QAENGPHLLV EAEQAKVFSH RGGNVTLPCK FYRDPTAFGS GIHKIRIKWT KLTSDYLKEV DVFVSMGYHK KTYGGYQGRV FLKGGSDSDA SLVITDLTLE DYGRYKCEVI EGLEDDTVVV ALDLQGVVFP YFPRLGRYNL NFHEAQQACL DQDAVIASFD QLYDAWRGGL DWCNAGWLSD GSVQYPITKP REPCGGQNTV PGVRNYGFWD KDKSRYDVFC FTSNFNGRFY YLIHPTKLTY DEAVQACLND GAQIAKVGQI FAAWKILGYD RCDAGWLADG SVRYPISRPR RRCSPTEAAV RFVGFPDKKH KLYGVYCFRA YN.

    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.

    Hapln1 Human
  • View Data Sheet

    Name :

    BECN1 Human

    Description:

    Beclin 1, Autophagy Related Human Recombinant

    ATG6, beclin1, VPS30, Coiled-coil myosin-like BCL2-interacting protein, Beclin-1, GT197.

    Product # :

    PRO-1289

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    Description

    BECN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 470 amino acids (1-450 a.a) and having a molecular mass of 54.1kDa.BECN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BECN1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BECN1, Beclin-1 and autophagy-related gene (Atg) 6, is a member of the beclin family. BECN1 has a key role in autophagy and antiviral host defense. Beclin-1 and its binding partner class III phosphoinositide 3-kinase (PI3K), also named Vps34, are vital for the initiation of the formation of the autophagasome in autophagy. Also it is required for the abscission step of cytokinesis.

    • Synonyms

      ATG6, beclin1, VPS30, Coiled-coil myosin-like BCL2-interacting protein, Beclin-1, GT197.

    • 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 MEGSKTSNNS TMQVSFVCQR CSQPLKLDTS FKILDRVTIQ ELTAPLLTTA QAKPGETQEE ETNSGEEPFI ETPRQDGVSR RFIPPARMMS TESANSFTLI GEASDGGTME NLSRRLKVTG DLFDIMSGQT DVDHPLCEEC TDTLLDQLDT QLNVTENECQ NYKRCLEILE QMNEDDSEQL QMELKELALE EERLIQELED VEKNRKIVAE NLEKVQAEAE RLDQEEAQYQ REYSEFKRQQ LELDDELKSV ENQMRYAQTQ LDKLKKTNVF NATFHIWHSG QFGTINNFRL GRLPSVPVEW NEINAAWGQT VLLLHALANK MGLKFQRYRL VPYGNHSYLE SLTDKSKELP LYCSGGLRFF WDNKFDHAMV AFLDCVQQFK EEVEKGETRF CLPYRMDVEK GKIEDTGGSG GSYSIKTQFN SEEQWTKALK FMLTNLKWGL AWVSSQFYNK.

    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.

    Becn1 Human
  • View Data Sheet

    Name :

    RCAN3 Human

    Description:

    Regulator of Calcineurin 3 Human Recombinant

    DSCR1L2, hRCN3, MCIP3, RCN3, Calcipressin-3, Down syndrome candidate region 1-like protein 2, Myocyte-enriched calcineurin-interacting protein 3, Regulator of calcineurin 3.

    Product # :

    PRO-1284

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    Description

    RCAN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 209 amino acids (56-241) and having a molecular mass of 23.5 kDa. RCAN3 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RCAN3 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 20% glycerol and 0.2M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcipressin-3 (RCAN3) takes part in central nervous system development. RCAN3 inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Overexpression of calcipressin-3 results in inhibition of calcineurin activity towards the nuclear factor of activated T-cells (NFAT) transcription factors and also downregulates NFAT-dependent cytokine gene expression in activated Jurkat T-cells. Highest expression takes place s in heart, skeletal muscle kidney, liver and peripheral blood leukocytes.

    • Synonyms

      DSCR1L2, hRCN3, MCIP3, RCN3, Calcipressin-3, Down syndrome candidate region 1-like protein 2, Myocyte-enriched calcineurin-interacting protein 3, Regulator of calcineurin 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 MGSEAVFEAR EQKERFEALF TIYDDQVTFQ LFKSFRRVRI NFSKPEAAAR ARIELHETDF NGQKLKLYFA QVQMSGEVRD KSYLLPPQPV KQFLISPPAS PPVGWKQSED AMPVINYDLL CAVSKLGPGE KYELHAGTES TPSVVVHVCE SETEEEEETK NPKQKIAQTR RPDPPTAALN EPQTFDCAL.

    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.

    Rcan3 Human
  • View Data Sheet

    Name :

    Bcl XL Human

    Description:

    B-Cell Lymphoma Extra Large Human Recombinant

    BclXL, Bcl-X(L), Bcl-XL.

    Product # :

    PRO-639

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    Description

    Bcl-XL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-210.The Bcl-XL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
      Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein.

    • Synonyms

      BclXL, Bcl-X(L), Bcl-XL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

      Suspend BclXL in 1000µl sterile 18M-cm H2O, over night at 4°C. Dilute 10 fold into selected buffer system.Bcl-XL has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.

    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.

    Bcl Xl Human
  • View Data Sheet

    Name :

    BLyS Human

    Description:

    B-cell Activating Factor Human Recombinant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-307

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    Description

    BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

    Purity

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

    Biological Activity

    The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 17.7kDa.

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

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

      What is the Biological Activity of BLYS Protein?
      The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

      What is the amino acid sequence of BLYS Protein?
      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

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

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

    Blys Human
  • View Data Sheet

    Name :

    Betacellulin Bovine

    Description:

    Betacellulin Bovine Recombinant

    Product # :

    CYT-406

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    Description

    Betacellulin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9003 Dalton. Betacellulin Bovine Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Betacellulin Bovine Recombinant was lyophilized after extensive dialysis against 50mM acetic acid.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Gly-Asn-Ser-Thr.

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9kDa.

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

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

      What is the Biological Activity of BETACELLULIN Protein?
      The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.

      What is the amino acid sequence of BETACELLULIN Protein?
      BETACELLULIN Protein is composed from 80 amino acids.

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

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

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.59 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). 2. Analysis by RP-HPLC, using a calibrated solution of BTC as a Reference Standard.

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

    Betacellulin Bovine
  • View Data Sheet

    Name :

    Bcl XL Mouse

    Description:

    B-Cell Leukemia/Lymphoma XL Mouse Recombinant

    BclXL, Bcl-X(L), Bcl-XL.

    Product # :

    PRO-1362

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    Description

    Bcl-XL Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids, having an MW of 23.7kDa.The Bcl-XL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Bcl-XL Mouse was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.

    Purity

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

    More Info

    • Introduction

      Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
      Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein.

    • Synonyms

      BclXL, Bcl-X(L), Bcl-XL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SQSNRELVVD FLSYKLSQKG YSWSQFSDVE ENRTEAPEET EAERETPSAI NGNPSWHLAD SPAVNGATGH SSSLDAREVI PMAAVKQALR EAGDEFELRY RRAFSDLTSQ LHITPGTAYQ SFEQVVNELF RDGVNWGRIV AFFSFGGALC VESVDKEMQV LVSRIASWMA TYLNDHLEPW IQENGGWDTF VDLYGNNAAA ESRKGQERFN R.

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

    Bcl Xl Mouse
  • View Data Sheet

    Name :

    CANT1 Human

    Description:

    Calcium Activated Nucleotidase 1 Human Recombinant

    Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    Product # :

    PRO-1010

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    Description

    CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.

    • Synonyms

      Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    • 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 MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.

    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.

    Cant1 Human
  • View Data Sheet

    Name :

    BLyS Human, His

    Description:

    B cell Activating Factor Human Recombinant, His Tag

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-545

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    • sds-page

    Description

    BLyS Human Recombinant fused to His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (134-285 a.a.) and having a molecular mass of 21 kDa. BAFF is fused to a 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Recombinant His Tag BAFF contains PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    BLyS-sds-page - Product image 1

    More Info

    • Introduction

      Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. a third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • 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 KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 21kDa.

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

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

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

      What is the amino acid sequence of BLYS Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL

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

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

    Blys Human His
  • View Data Sheet

    Name :

    Bcl XL Human, His

    Description:

    B-Cell Lymphoma Extra Large Human Recombinant, His Tag

    BclXL, Bcl-X(L), Bcl-XL.

    Product # :

    PRO-641

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Bcl-XL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-210.The Bcl-XL is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 10mM Tris-HCL pH-8, 1mM EDTA and 250mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bcl-XL is a transmembrane protein located in the mitochondrial membranes of cells that are long-lived and postmitotic, such as adult brain cells. It plays arole in the signal transduction pathway of the FAS-Ligand. Bcl-XL is an anti-apoptotic protein which is a member of the Bcl-2 family which are able to form heterodimers, and this is an significant event in the regulation of apoptosis. BCL-XL is involved in the survival of cancer cells.
      Bcl-xL is the leading monitor of apoptosis/active cell suicide. Bcl-xL has cell death repressor activity and therefore acts as a survival protein.

    • Synonyms

      BclXL, Bcl-X(L), Bcl-XL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

      Suspend BclXL in 100?l of 0.5M Acetic acid, over night at 4°C.
      Dilute 10 fold into selected buffer system.
      Bcl-XL has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.

    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.

    Bcl Xl Human His
  • View Data Sheet

    Name :

    BLyS Human, Plant

    Description:

    BAFF (BLyS) Human Recombinant, Plant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-054

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.

    Purity

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

    Biological Activity

    The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
    *activity results may vary with PBMC donors.
    ED50 ? 50ng/ml

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 19kDa.

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

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

      What is the Biological Activity of BLYS Protein?
      The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.

      What is the amino acid sequence of BLYS Protein?
      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

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

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

    Baff Human Plant
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