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1000 results found for “fibronectin”

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  • View Data Sheet

    Name :

    STC 1 Human

    Description:

    Stanniocalcin-1 Human Recombinant

    Stanniocalcin-1, STC, STC-1.

    Product # :

    HOR-259

    Price :

    Quantity :

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    Shipped at Room temp

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    Description

    Stanniocalcin-1 Human Recombinant produced in 293 cell line is a single, glycosylated, polypeptide chain containing 240 amino acids and having a total molecular mass of 25.9 kDa. The Stanniocalcin contains 10 residues form the C-Terminal Flag- tag. Stanniocalcin is purified by proprietary chromatographic techniques.

    Source

    293 cell line (Human embryonic kidney).

    Formulation

    Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stanniocalcin 1 (STC1) is the mammalian homologue of STC, which was originally identified as a calcium/phosphate-regulating hormone in bony fishes. In contrast, STC1 may play an autocrine and paracrine role with pleiotropic effects in mammals. It is expressed in a wide variety of tissues, but unexpectedly is not detected in the circulation under normal circumstances, which is possibly caused by its attaching to soluble and tethered forms of a high-affinity binding protein. STC-1 can affect calcium homeostasis, bone and muscle mass and structure, and angiogenesis through effects on osteoblasts, osteoclasts, myoblasts/myocytes, and endothelial cells in mouse model. Differential regulation of myocardial STC1 protein expression was reported in heart failure. In addition, STC1 may regulate calcium currents in cardiomyocytes and may contribute to the alterations in calcium homeostasis of the failing heart. STC1 was found to be a selective modulator of hepatocyte growth factor (HGF)-induced endothelial migration and morphogenesis, an inhibitor of macrophage chemotaxis and chemokinesis, suppressor of progesterone and luteinization inhibitor. Together with STC-2, it may play important roles in the processes of implantation and decidualization in the rat. In terminally differentiated adipocytes, it may function as a "survival factor", which contributes to the maintenance of the integrity of mature adipose tissue. In context with its possible role in gestation, a Big STC, a three highermolecular- mass variant has been described. STC1 was identified as one of hypoxia-responsive genes coupled to hypoxia-driven angiogenesis.
      Current research indicates that STC-1 might be a useful molecular marker to detect tumor cells in blood and bone marrow from patients with various types of malignancies.

    • Synonyms

      Stanniocalcin-1, STC, STC-1.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized STC-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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

      Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      THEAEQNDSV SPRKSRVAAQ NSAEVVRCLN SALQVGCGAF ACLENSTCDT DGMYDICKSF LYSAAKFDTQ GKAFVKESLK CIANGVTSKV FLAIRRCSTF QRMIAEVQEE CYSKLNVCSI AKRNPEAITE VVQLPNHFSN RYYNRLVRSL LECDEDTVST IRDSLMEKIG PNMASLFHIL QTDHCAQTHP RADFNRRRTN EPQKLKVLLR NLRGEEDSPS HIKRTSHESA ASDYKDDDDK.

    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.

    Stc 1 Human
  • View Data Sheet

    Name :

    TRIM21 Human Biotin

    Description:

    Tripartite Motif Containing 21 (RO52) Human Recombinant, Biotinylated

    52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    Product # :

    PRO-2559

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    • description
    • source
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    • More Info

    Description

    TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa. TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TRIM21 solution is supplied in 20mM HEPES pH-7.6, 0.01mM EDTA and 0.02% SDS.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

    • Synonyms

      52 kDa Ro protein, Sjoegren syndrome type A antigen, SS-A, Ro(SS-A), 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Tripartite motif-containing protein 21, RING finger protein 81, TRIM21, RNF81, RO52, SSA1, SSA, RO-52.

    • 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 IgG type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

    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.

    Ro52 Human
  • View Data Sheet

    Name :

    ACVR1 Human

    Description:

    Activin A Receptor Type 1 Human Recombinant

    ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.

    Product # :

    CYT-1140

    Price :

    Quantity :

    Shipping Method :

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    • sds-page

    Description

    ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACVR1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    ACVR1 Human sds-page - Product image 1

    More Info

    • Introduction

      Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.

    • Synonyms

      ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.

    • 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

      MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
      CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
      PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
      REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
      PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
      VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

    • Background

      Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant

      1. Abstract

      This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.

      2. Introduction

      The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.

      3. Structure and Signaling of ACVR1

      ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.

      4. Biological Functions of ACVR1

      Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.

      5. ACVR1 in Disease Pathology

      The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.

      6. Therapeutic Potential of ACVR1

      Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.

      7. Conclusion and Future Perspectives

      While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.

      What is the molecular weight / Mw of ACVR1 Protein?
      ACVR1 Protein has a total Mw of 38.4kDa.

      What is the source or expression system of ACVR1 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of ACVR1 Protein?
      ACVR1 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of ACVR1 Protein?
      The biological functionality of ACVR1 Protein will be determined in the future.

      What is the endotoxin level for ACVR1 Protein?
      The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACVR1 Protein?
      MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
      CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
      PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
      REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
      PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
      VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

      What applications can ACVR1 Protein be used in?
      ACVR1 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.

    Acvr1 Human
  • View Data Sheet

    Name :

    SNCA Human

    Description:

    Alpha Synuclein Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-393

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    Description

    a-Synuclein Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (Real molecular weight on SDS-PAGE will be shift up). The Recombinant Human a-Synuclein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl and 1mM MgCl2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

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    Snca Human
  • View Data Sheet

    Name :

    LMNA Rat

    Description:

    Lamin A/C Rat Recombinant

    Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    Product # :

    PRO-2667

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    Description

    LMNA Rat Recombinant fused with a His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 614 amino acids and having a molecular mass of 68.0kDa. The LMNA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LMNA solution contains 20mM Tris-HCl pH 7.5, 1mM DTT, 0.3M NaCl, 1.5mM EDTA and 10%(v/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
      Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
      Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.

    • Synonyms

      Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    • 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

      METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN TKKEGDLLAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQSQ GGGSVTKKRK LESSESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIR RQNGDDPLMT YRFPPKFTLK AGQVVTIWAS GAGATHSPPT DLVWKAQNTW GCGSSLRTAL INATGEEVAM RKLVRSLTMV EDDEDEDGDD LLHHHHGSHC SSSGDPAEYN LRSRTVLCGT CGQPADKASA SGSGAQVSSQ NCSIM

    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.

    Lmna Rat
  • View Data Sheet

    Name :

    FGF 2 Bovine

    Description:

    Fibroblast Growth Factor-Basic Bovine Recombinant

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

    Product # :

    CYT-288

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    Description

    FGF-2 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17250 Dalton. The Fibroblast Growth Factor 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF-b Bovine was lyophilized from a concentrated (1mg/ml) sterile solution containing 1% HSA.

    Purity

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

    Biological Activity

    The ED50, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be <0.1ng/ml, corresponding to a specific activity of 3 x 106 Units/mg.

    More Info

    • Introduction

      FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
      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

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fibroblast Growth Factor 2 Bovine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-b Bovine Recombinant 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 Fibroblast Growth Factor-2 Bovine Recombinant 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 Met-Ala-Ala-Gly-Ser.

    • Background

      What is the molecular weight/Mw of FGF-2 BOVINE Protein?
      FGF-2 BOVINE Protein has a total Mw of 17.5kDa.

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

      What is the Purity of FGF-2 BOVINE Protein?
      FGF-2 BOVINE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF-2 BOVINE Protein?
      The ED50, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be <0.1ng/ml, corresponding to a specific activity of 3 x 106 Units/mg.

      What is the amino acid sequence of FGF-2 BOVINE Protein?
      FGF-2 BOVINE Protein is composed from 155 amino acids.

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

      What is the endotoxin level for FGF-2 BOVINE Protein?
      The endotoxin level is minimal, FGF-2 BOVINE 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 0.85 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 FGF-2 Bovine 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.

    Fgf 2 Bovine Recombinant
  • View Data Sheet

    Name :

    LGALS13 Human

    Description:

    Galectin-13 Human Recombinant

    Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.

    Product # :

    CYT-004

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    Description

    Recombinant Human LGALS13 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 16kDa. The LGALS13 also might appear as a homodimer, having a total Mw of 32kDa. LGALS13 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    LGALS13 protein solution (0.5mg/ml) is formulated in 1xPBS buffer pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Galectin-13 is an E. coli expressed peptide, this protein is one of human placenta specific galectins, like all galectin family, it contains a carbohydrate recognition domain (CRD) as well. Increased blood concentration was found highly asscoaited with preeclampsia and HELLP syndrome in pregnant women. The molecular weight of galectin-13 is 16kDa.

    • Synonyms

      Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.

    • 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

      MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK

      QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN

    • Background

      What is the molecular weight/Mw of LGALS13 HUMAN Protein?
      LGALS13 HUMAN Protein has a total Mw of 32kDa.

      What is the source or expression system of LGALS13 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS13 HUMAN Protein?
      LGALS13 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS13 HUMAN Protein?
      The biological functionality of LGALS13 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of LGALS13 HUMAN Protein?
      MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK
      QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN

      What applications can LGALS13 HUMAN Protein be used in?
      LGALS13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS13 HUMAN Protein?
      The endotoxin level is minimal, LGALS13 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.

    Lgals13 Human
  • View Data Sheet

    Name :

    FCGR2A Human, HEK

    Description:

    CD32a Human Recombinant, HEK

    CD32, CD32A, CDw32, FcGR, IGFR2, MGC23887, MGC30032, Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a, Fc-gamma-RIIa, FcRII-a, FCG2, FCGR2A1.

    Product # :

    PRO-2775

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    Description

    FCGR2A Human Recombinant is a single, glycosylated, polypeptide chain (30-218 a.a) containing a total of 195 amino acids, having a molecular mass of 21.6kDa. FCGR2A is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    FCGR2A protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤5 ug/ml. and is measured by its binding ability in a functional ELISA with Human IgG1 Fc (CAT# pro-2763). 

    More Info

    • Synonyms

      CD32, CD32A, CDw32, FcGR, IGFR2, MGC23887, MGC30032, Low affinity immunoglobulin gamma Fc region receptor II-a, IgG Fc receptor II-a, Fc-gamma-RIIa, FcRII-a, FCG2, FCGR2A1.

    • 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

      SADSQAAAPP KAVLKLEPPW INVLQEDSVT LTCQGARSPE SDSIQWFHNG NLIPTHTQPS YRFKANNNDS GEYTCQTGQT SLSDPVHLTV LSEWLVLQTP HLEFQEGETI MLRCHSWKDK PLVKVTFFQN GKSQKFSHLD PTFSIPQANH SHSGDYHCTG NIGYTLFSSK PVTITVQVPS MGSSSPMGIH HHHHH.

    • Background

      The immune system is a complex network of cells and molecules that play a crucial role in protecting the body against pathogens and maintaining homeostasis. Fc gamma receptors (FcγRs) are a family of cell surface receptors that mediate the effector functions of antibodies, particularly immunoglobulin G (IgG). Among these receptors, FCGR2A, also known as CD32a, is a prominent member expressed on the surface of various immune cells. This research aims to investigate the structure, function, and implications of FCGR2A protein in immune responses, with a focus on its relevance to human health and therapeutic applications.

      Structure and Expression of FCGR2A:

      FCGR2A is a transmembrane glycoprotein composed of two extracellular immunoglobulin-like domains, a transmembrane domain, and a cytoplasmic tail. It is primarily expressed on immune cells such as macrophages, monocytes, and dendritic cells. The unique structure of FCGR2A allows it to bind to the Fc portion of IgG antibodies, initiating immune effector functions.

      Role of FCGR2A in Immune Responses:

      FCGR2A plays a crucial role in modulating immune responses through its involvement in antibody-dependent cellular cytotoxicity (ADCC) and phagocytosis. Upon binding to IgG antibodies, FCGR2A triggers intracellular signaling cascades that activate immune effector cells, leading to the elimination of antibody-bound pathogens or targeted cells. Furthermore, FCGR2A is involved in immune complex clearance, regulation of cytokine production, and modulation of cellular activation, thus contributing to the overall immune response.

      Implications of FCGR2A in Human Health:

      The dysregulation of FCGR2A has been implicated in various immune-related diseases. Genetic variations in FCGR2A have been associated with increased susceptibility to autoimmune disorders, such as systemic lupus erythematosus and rheumatoid arthritis. Altered FCGR2A expression or function has also been observed in infectious diseases, including HIV and malaria, affecting disease progression and immune control. Understanding the role of FCGR2A in these conditions is crucial for developing targeted therapeutic strategies.

      Therapeutic Potential of FCGR2A:

      The unique properties of FCGR2A make it an attractive target for therapeutic interventions. Modulating FCGR2A activity and function can potentially enhance immune responses against pathogens or tumor cells. For example, monoclonal antibodies that target FCGR2A have shown promising results in cancer immunotherapy by promoting ADCC and phagocytosis of tumor cells. Furthermore, strategies aimed at selectively activating or inhibiting FCGR2A signaling could lead to the development of novel immunotherapeutic approaches.

      Challenges and Future Perspectives:

      While the study of FCGR2A holds great promise, several challenges need to be addressed. Further research is required to unravel the intricate interplay between FCGR2A and other immune receptors and signaling molecules. Additionally, the development of therapeutic agents that selectively target FCGR2A without compromising normal immune functions remains a challenge.

      Conclusion:

      The investigation of FCGR2A protein provides insights into its pivotal role in immune responses and its implications for human health and therapeutics. Understanding the structure, function, and dysregulation of FCGR2A in immune-related diseases opens avenues for the development of targeted therapies. Continued research on FCGR2A and its interactions within the immune system will contribute to advancements in immunotherapy and personalized medicine.

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    Fcgr2A Human Hek
  • View Data Sheet

    Name :

    FUT7 Human

    Description:

    Fucosyltransferase 7 Human Recombinant

    Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    Product # :

    ENZ-784

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    Description

    FUT7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (37-342) and having a molecular mass of 37.9kDa.FUT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FUT7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fucosyltransferase 7 (FUT7) is a golgi stack membrane protein which is involved in the creation of sialyl-Lewis X antigens. The FUT7 protein leads the synthesis of the E-selectin-binding sialyl-Lewis X moiety. FUT7 catalyzes alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens.

    • Synonyms

      Fucosyltransferase 7 (Alpha (1,3) Fucosyltransferase), Fucosyltransferase VII, Galactoside 3-L-Fucosyltransferase, Selectin Ligand Synthase, FucT-VII, Fuc-TVII, FUT7, Alpha-(1,3)-Fucosyltransferase 7, Selectin-Ligand Synthase, EC 2.4.1.-, Fuc-TVII, Fucosyltransferase 7, EC 2.4.1, EC 2.4.1.65.

    • 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 MGSPRGTPAP QPTITILVWH WPFTDQPPEL PSDTCTRYGI ARCHLSANRS LLASADAVVF HHRELQTRRS HLPLAQRPRG QPWVWASMES PSHTHGLSHL RGIFNWVLSY RRDSDIFVPY GRLEPHWGPS PPLPAKSRVA AWVVSNFQER QLRARLYRQL APHLRVDVFG RANGRPLCAS CLVPTVAQYR FYLSFENSQH RDYITEKFWR NALVAGTVPV VLGPPRATYE AFVPADAFVH VDDFGSAREL AAFLTGMNES RYQRFFAWRD RLRVRLFTDW RERFCAICDR YPHLPRSQVY EDLEGWFQA.

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    Fut7 Human
  • View Data Sheet

    Name :

    VTCN1 Human, Sf9

    Description:

    V-Set Domain Containing T Cell Activation Inhibitor 1 Human Recombinant, Sf9

    V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    Product # :

    PRO-2439

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    Description

    VTCN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 244 amino acids (25-259a.a.) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). VTCN1 is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VTCN1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.

    • Synonyms

      V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    • 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).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPLIIGFGI SGRHSITVTT VASAGNIGED GILSCTFEPD IKLSDIVIQW LKEGVLGLVH EFKEGKDELS EQDEMFRGRT AVFADQVIVG NASLRLKNVQ LTDAGTYKCY IITSKGKGNA NLEYKTGAFS MPEVNVDYNA SSETLRCEAP RWFPQPTVVW ASQVDQGANF SEVSNTSFEL NSENVTMKVV SVLYNVTINN TYSCMIENDI AKATGDIKVT ESEIKRRSHL QLLNSKASHH HHHH.

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    Vtcn1 Protein
  • View Data Sheet

    Name :

    MEK1 Human

    Description:

    Mitogen Activated Kinase Kinase 1 Human Recombinant

    Product # :

    PKA-256

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    Description

    MAP2K1 active Human Recombinant produced in Sf9 cells is a glycosylated, polypeptide chain containing amino acids 2-393 having a molecular mass of 47 kDa. MAP2K1 is fused to a polyhistidine tag and is purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    MEK1 is supplied at a concentration of in 40mM Tris, pH-8, 0.15M NaCl, 0.27M sucrose, 1mM DTT, 0.2mM PMSF, 1mM benzamidine, 0.1mM sodium vanadate and 0.03% Brij-35.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    ~125-175 units/mg. One unit of MEK1 activity transfers 1 nmol of phosphate to ERK1/2 peptide per minute at 30°C in a reaction containing 100µM ATP.
    Recombinant active MEK1 also phosphorylates ERK1, ERK2, and GSK-3?. Kinase activity may vary depending on the substrate and reaction conditions.
    The optimal concentration should be determined for each specific application.

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    • Introduction

      MAP2K1 is a member of the dual specificity protein kinase family, which plays a role as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, are recognized as extracellular signal-regulated kinases (ERKs), that act as an integration position for multiple biochemical signals. MEK1 is located upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon wide variety of extra- and intracellular signals. As a key player of MAP kinase signal transduction pathway, MEK1 is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development. MAP2K1 catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a thr-glu-tyr sequence located in map kinases. MEK1 activates erk1 and erk2 map kinases.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 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.

    Mek1 Human
  • View Data Sheet

    Name :

    ODC1 antibody

    Description:

    Ornithine Decarboxylase 1, Mouse Anti Human

    ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    Product # :

    ANT-739

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    Formulation

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

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    • Introduction

      Ornithine decarboxylase is the preliminary and rate-limiting enzyme in the biosynthetic pathway of polyamines and it takes part in the alteration of ornithine to putrescine. ODC1 is a key member of various biological processes, such as cell growth, transformation, differentiation and apoptosis. Overexpression of the ODC1 gene has a vital part in cell proliferation and the progress of cancer.

    • Synonyms

      ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human ODC1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ODC1 amino acids 1-461 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT9B3AT.

    • Applications

      ODC1 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

      ODC1 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.

    Odc1 Antibody
  • View Data Sheet

    Name :

    FABP3 Paired Antibody

    Description:

    Mouse Anti Human Fatty Acid Binding Protein-3 Paired

    Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    Product # :

    ANT-723

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    Description

    FABP3 gold conjugation antibody and FABP3 capture antibody are used to develop rapid test for FABP3 rapid test. Please note that when ordering for example: 50µg antibody we ship 25µg from each of the antibodies (50µg in total).

    Formulation

    * FABP3 gold conjugation antibody in PBS and NaN3.

    * FABP3 capture antibody.

    Purity

    Greater than 95%.

    More Info

    • Introduction

      Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.

    • Synonyms

      Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    • Physical Appearance

      2 vials of sterile Filtered clear colorless solution.

    • Applications

      Lateral flow immunoassay.

    • Type

      Mouse Anti Human Monoclonal.

    • Purification Method

      Purified monoclonal IgG by protein A 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.

    Fabp3 Paired Antibody
  • View Data Sheet

    Name :

    ICAM1 Human, Sf9

    Description:

    Intercellular Adhesion Molecule-1 Human Recombinant, SF9

    Intercellular Adhesion Molecule 1, Major Group Rhinovirus Receptor, ICAM-1, Intercellular Adhesion Molecule 1 (CD54), Human Rhinovirus Receptor, Cell Surface Glycoprotein P3.58, Human Rhinovirus Receptor, CD54 Antigen, P3.58, CD54, BB2, Intercellular adhesion molecule 1.

    Product # :

    PRO-2200

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    Description

    ICAM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 692 amino acids (28-480a.a.) and having a molecular mass of 76.5kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ICAM1 is expressed with a 239 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ICAM1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 2 ug/ml is measured by the ability of the immobilized protein to support the adhesion of HL-60 human promyelocytic cells. When cells are added to Human ICAM-1/CD54 coated plates.

    More Info

    • Introduction

      ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues. ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH. Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions.

    • Synonyms

      Intercellular Adhesion Molecule 1, Major Group Rhinovirus Receptor, ICAM-1, Intercellular Adhesion Molecule 1 (CD54), Human Rhinovirus Receptor, Cell Surface Glycoprotein P3.58, Human Rhinovirus Receptor, CD54 Antigen, P3.58, CD54, BB2, Intercellular adhesion molecule 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      QTSVSPSKVI LPRGGSVLVT CSTSCDQPKL LGIETPLPKK ELLLPGNNRK VYELSNVQED SQPMCYSNCP DGQSTAKTFL TVYWTPERVE LAPLPSWQPV GKNLTLRCQV EGGAPRANLT VVLLRGEKEL KREPAVGEPA EVTTTVLVRR DHHGANFSCR TELDLRPQGL ELFENTSAPY QLQTFVLPAT PPQLVSPRVL EVDTQGTVVC SLDGLFPVSE AQVHLALGDQ RLNPTVTYGN DSFSAKASVS VTAEDEGTQR LTCAVILGNQ SQETLQTVTI YSFPAPNVIL TKPEVSEGTE VTVKCEAHPR AKVTLNGVPA QPLGPRAQLL LKATPEDNGR SFSCSATLEV AGQLIHKNQT RELRVLYGPR LDERDCPGNW TWPENSQQTP MCQAWGNPLP ELKCLKDGTF PLPIGESVTV TRDLEGTYLC RARSTQGEVT REVTVNVLSP RYEVEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYRQKSL SLSPGKHHHH HH.

    • Background

      Intercellular adhesion molecule-1 (ICAM-1) is a cell surface glycoprotein that plays a pivotal role in immune responses and inflammatory processes. This research aims to investigate the function and significance of ICAM-1 protein in various physiological and pathological conditions. Understanding the molecular mechanisms and regulatory roles of ICAM-1 can provide valuable insights into its potential as a therapeutic target for immune-related disorders.

      Structure and Expression of ICAM-1 Protein:

      ICAM-1 belongs to the immunoglobulin superfamily and is composed of five immunoglobulin-like domains. It is primarily expressed on the surfaces of endothelial cells, leukocytes, and other immune cells. ICAM-1 expression can be induced by pro-inflammatory cytokines, such as tumor necrosis factor-alpha (TNF-α) and interleukin-1 (IL-1), during immune responses and inflammatory conditions.

      ICAM-1 and Leukocyte Adhesion:

      One of the critical functions of ICAM-1 is its involvement in leukocyte adhesion and migration. ICAM-1 interacts with its primary receptor, lymphocyte function-associated antigen-1 (LFA-1), expressed on leukocytes. This interaction facilitates the firm adhesion of leukocytes to endothelial cells, leading to their transmigration into inflamed tissues. The ICAM-1/LFA-1 axis plays a crucial role in immune surveillance, inflammation, and host defense against pathogens.

      Implications of ICAM-1 in Inflammatory Disorders:

      ICAM-1 has been implicated in various inflammatory diseases, including rheumatoid arthritis, inflammatory bowel disease, and multiple sclerosis. Enhanced expression of ICAM-1 on endothelial cells promotes leukocyte recruitment and contributes to the perpetuation of chronic inflammation. Therefore, targeting ICAM-1-mediated leukocyte adhesion has emerged as a potential therapeutic strategy to alleviate inflammation and attenuate disease progression.

      ICAM-1 in Viral Infections:

      ICAM-1 also plays a role in viral infections, as several viruses exploit ICAM-1 to facilitate their entry into host cells. For instance, rhinoviruses, which cause the common cold, utilize ICAM-1 as a receptor for attachment and entry into respiratory epithelial cells. The interaction between ICAM-1 and viral proteins promotes viral internalization and subsequent infection. Understanding the mechanisms of ICAM-1-mediated viral entry can aid in the development of antiviral strategies.

      Therapeutic Targeting of ICAM-1:

      Given its crucial involvement in immune responses and disease pathogenesis, ICAM-1 has emerged as a potential therapeutic target. Strategies aimed at blocking ICAM-1/LFA-1 interactions have shown promise in preclinical and clinical studies. Monoclonal antibodies targeting ICAM-1 or LFA-1 have been developed to prevent leukocyte adhesion and reduce inflammation. Additionally, small molecule inhibitors and gene therapies targeting ICAM-1 expression are being explored as potential therapeutic interventions.

      Challenges and Future Directions:

      Although therapeutic targeting of ICAM-1 shows promise, several challenges need to be addressed. Specific targeting of ICAM-1 without affecting its physiological functions and potential off-target effects are important considerations. Additionally, the complex and dynamic nature of ICAM-1 expression and regulation require further investigation to optimize therapeutic strategies.

      Conclusion:

      The investigation of ICAM-1 protein provides insights into its pivotal role in immune responses, leukocyte adhesion, and inflammatory processes. Understanding the molecular mechanisms and functional implications of ICAM-1 opens avenues for the development of targeted therapies for inflammatory disorders and viral infections. Further research on ICAM-1 protein

    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.

    Icam1 Human Sf9
  • View Data Sheet

    Name :

    GMFB Human

    Description:

    Glia Maturation Factor Beta Human Recombinant

    Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    Product # :

    CYT-565

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    Description

    Glia Maturation Factor-Beta (GMF-Beta) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.5 kDa. Glia Maturation Factor-Beta, GMF-Beta, Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMF-beta protein was lyophilized after dialysis against 20mM PBS pH=7.4 and 130mM NaCl.

    Purity

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

    More Info

    • Introduction

      Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
      Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
      GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
      GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.

    • Synonyms

      Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
      ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
      KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

    • Background

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

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

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

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

      What is the amino acid sequence of GMFB HUMAN Protein?
      SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
      ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
      KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

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

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

    Gmfb Human
  • View Data Sheet

    Name :

    SNCA E46K, Human

    Description:

    Alpha-Synuclein E46K Human Recombinant

    SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.

    Product # :

    PRO-2626

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    Description

    SNCA E46K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140a.a.) and having a molecular mass of 14.4kDa.SNCA is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SNCA protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 7.5) and 0.1 M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNCA or Alpha-synuclein is a protein with undisclosed function that mainly concentrated in the brain tissue, mainly in the tips of the neurons in the presynaptic terminals. Almost 1% of the proteins in the brain tissues are synucleins. The protein is located mainly in the hippocampus, thalamus, cerebellum & neocortex. Smaller amounts of the SNCA protein can be found in the neuroglial cells. The MITF protein regulates the SNCA expression in melanocytic cells.

    • Synonyms

      SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKKGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA

    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.

    Synuclein Alpha
  • View Data Sheet

    Name :

    SURF2 Human

    Description:

    Surfeit-2 Human Recombinant

    Surfeit 2, SURF-2, SURF2, Surfeit locus protein 2, Surfeit-2.

    Product # :

    PRO-1470

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    Description

    SURF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-256) and having a molecular mass of 32 kDa. SURF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SURF2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Surfeit-2 (SURF2) is a member of the SURF2 family. SURF2 interacts with beta-1, 4-Gal-T3, uPAR and WDR20. SURF2 is located in the surfeit gene cluster, a group of extremely tightly linked genes that don't share sequence similarity. The SURF2 gene maps to human chromosome 9q34.2 and shares a bidirectional promoter with SURF1 that is found on the opposite strand. The intergenic region between the SURF1 and SURF2 genes is expected to have bidirectional promoter activity, as is found in mice.

    • Synonyms

      Surfeit 2, SURF-2, SURF2, Surfeit locus protein 2, Surfeit-2.

    • 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 MGSMSELPGD VRAFLREHPS LRLQTDARKV RCILTGHELP CRLPELQVYT RGKKYQRLVR ASPAFDYAEF EPHIVPSTKN PHQLFCKLTL RHINKCPEHV LRHTQGRRYQ RALCKYEECQ KQGVEYVPAC LVHRRRRRED QMDGDGPRPR EAFWEPTSSD EGGAASDDSM TDLYPPELFT RKDLGSTEDG DGTDDFLTDK EDEKAKPPRE KATDEGRRET TVYRGLVQKR GKKQLGSLKK KFKSHHRKPK SFSSCKQPG.

    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.

    Surf2 Human
  • View Data Sheet

    Name :

    CAPNS1 Antibody

    Description:

    Calpain, Small Subunit 1, Mouse Anti Human

    Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    Product # :

    ANT-587

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    • More Info

    Formulation

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

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    • Introduction

      Calpain, Small Subunit 1 (CAPNS1) belongs to the calpain small subunit family. Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases, widely distributed in mammalian cells. Calpain families are implicated in neurodegenerative processes, considering that their activation can be triggered by calcium influx and oxidative stress. Calpains function as heterodimers, comprising a specific large catalytic subunit (calpain 1 subunit in Calpain I, and calpain 2 subunit in Calpain II), and a common small regulatory subunit encoded by the CAPNS1 gene. The CAPNS1 protein is vital for the stability and function of both calpain heterodimers, whose proteolytic activities influence numerous cellular functions including apoptosis, proliferation, migration, adhesion, and autophagy.

    • Synonyms

      Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CAPNS1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CAPNS1 protein 84-268 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1D11AT.

    • Applications

      CAPNS1 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry 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

      CAPNS1 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.

    Capns1 Antibody
  • View Data Sheet

    Name :

    ADRM1 Human

    Description:

    Adhesion Regulating Molecule 1 Human Recombinant

    Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.

    Product # :

    PRO-1079

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    Description

    ADRM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 431 amino acids (1-407 a.a) and having a molecular mass of 44.7kDa.ADRM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ADRM1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proteasomal ubiquitin receptor ADRM1 (ADRM1) functions as a proteasomal ubiquitin receptor. ADRM1 is an integral plasma membrane protein which promotes cell adhesion. ADRM1 is assumed to undergo O-linked glycosylation. ADRM1 employs the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.

    • Synonyms

      Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.

    • 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 MGSHMTTSGA LFPSLVPGSR GASNKYLVEF RAGKMSLKGT TVTPDKRKGL VYIQQTDDSL IHFCWKDRTS GNVEDDLIIF PDDCEFKRVP QCPSGRVYVL KFKAGSKRLF FWMQEPKTDQ DEEHCRKVNE YLNNPPMPGA LGASGSSGHE LSALGGEGGL QSLLGNMSHS QLMQLIGPAG LGGLGGLGAL TGPGLASLLG SSGPPGSSSS SSSRSQSAAV TPSSTTSSTR ATPAPSAPAA ASATSPSPAP SSGNGASTAA SPTQPIQLSD LQSILATMNV PAGPAGGQQV DLASVLTPEI MAPILANADV QERLLPYLPS GESLPQTADE IQNTLTSPQF QQALGMFSAA LASGQLGPLM CQFGLPAEAV EAANKGDVEA FAKAMQNNAK PEQKEGDTKD KKDEEEDMSL D.

    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.

    Adrm1 Human
  • View Data Sheet

    Name :

    AFP Protein

    Description:

    Alpha Fetoprotein Human Recombinant

    Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.

    Product # :

    PRO-2229

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    Description

    AFP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 600 amino acids (19-609a.a.) and having a molecular mass of 67.5kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). AFP is expressed with a ADP at N-terminus and 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.

    • Synonyms

      Alpha-Fetoprotein, Alpha-1-Fetoprotein, Alpha-Fetoglobulin, HPAFP, AFPD, FETA, HP, Alpha-fetoprotein.

    • 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

      ADPRTLHRNEYGI ASILDSYQCT AEISLADLAT IFFAQFVQEA TYKEVSKMVK DALTAIEKPT GDEQSSGCLE NQLPAFLEEL CHEKEILEKY GHSDCCSQSE EGRHNCFLAH KKPTPASIPL FQVPEPVTSC EAYEEDRETF MNKFIYEIAR RHPFLYAPTI LLWAARYDKI IPSCCKAENA VECFQTKAAT VTKELRESSL LNQHACAVMK NFGTRTFQAI TVTKLSQKFT KVNFTEIQKL VLDVAHVHEH CCRGDVLDCL QDGEKIMSYI CSQQDTLSNK ITECCKLTTL ERGQCIIHAE NDEKPEGLSP NLNRFLGDRD FNQFSSGEKN IFLASFVHEY SRRHPQLAVS VILRVAKGYQ ELLEKCFQTE NPLECQDKGE EELQKYIQES QALAKRSCGL FQKLGEYYLQ NAFLVAYTKK APQLTSSELM AITRKMAATA ATCCQLSEDK LLACGEGAAD IIIGHLCIRH EMTPVNPGVG QCCTSSYANR RPCFSSLVVD ETYVPPAFSD DKFIFHKDLC QAQGVALQTM KQEFLINLVK QKPQITEEQL EAVIADFSGL LEKCCQGQEQ EVCFAEEGQK LISKTRAALG VHHHHHH.

    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.

    Afp Human
  • View Data Sheet

    Name :

    ASS1 Human

    Description:

    Argininosuccinate Synthase 1 Human Recombinant

    ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.

    Product # :

    ENZ-548

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    Description

    ASS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 432 amino acids (1-412 a.a.) and having a molecular mass of 48.6 kDa. The ASS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ASS1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.

    • Synonyms

      ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF IEDVSREFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG KGNDQVRFEL SCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKNPWS MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNTP DILEIEFKKG VPVKVTNVKD GTTHQTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVLKGQVYI LGRESPLSLY NEELVSMNVQ GDYEPTDATG FININSLRLK EYHRLQSKVT AK.

    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.

    Ass1 Human
  • View Data Sheet

    Name :

    ECSIT Human

    Description:

    ECSIT homolog Human Recombinant

    ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.

    Product # :

    PRO-1241

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    Description

    ECSIT Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (19-217) and having a molecular mass of 24.6 kDa.ECSIT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ECSIT homolog (ECSIT) is a ubiquitously expressed protein which has a vital role as an adaptor protein in the cytosolic signal transduction cascade events triggered by Toll receptor activation. ECSIT promotes proteolytic activation of MAP3K1. ECSIT is also involved in the BMP signaling pathway. ECSIT is essential for normal embryonic development. ECSIT was originally classified as a cytoplasmic protein interacting specifically with TNF receptor associated factor (TRAF)-6 in the TLR pathway. ECSIT gene knockdown results in gravely impaired complex I assembly and disrupted mitochondrial function.

    • Synonyms

      ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.

    • 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 MGSGTCGAAL TGTSISQVPL PKDSTGAADP PQPHIVGIQS PDQQAALARH NPARPVFVEG PFSLWLRNKC VYYHILRADL LPPEEREVEE TPEEWNLYYP MQLDLEYVRS GWDNYEFDIN EVEEGPVFAM CMAGAHDQAT MAKWIQGLQE TNPTLAQIPV VFRLAGSTRE LQTSSAGLEE PPLPEDHQEE DDNLQRQQQG QS

    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.

    Ecsit Human
  • View Data Sheet

    Name :

    SOST Human

    Description:

    Sclerostin Human Recombinant

    Sclerostin, SOST, CDD, VBCH.

    Product # :

    PRO-1601

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    Description

    SOST Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 24-213) containing 200 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 22.8kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.03M Acetate buffer pH-4.0.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      Sclerostin, SOST, CDD, VBCH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASQGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY.

    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.

    Sost Human
  • View Data Sheet

    Name :

    FABP5 Human, His

    Description:

    Fatty Acid Binding Protein 5 Human Recombinant, His Tag

    Fatty acid-binding protein epidermal, E-FABP, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, PA-FABP, FABP5, EFABP, PAFABP.

    Product # :

    PRO-666

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    Description

    FABP5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 19.66kDa. FABP5 is fused to His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP5 His-Tag is supplied in 20mM Tris HCl pH-8 and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Human Fatty Epidermal Acid Binding Protein FABP also called FABP-5 is a 15 kD member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds ( bile acids or retinoids). In an internal cavity. The fatty acid binding proteins aP2 (fatty acid binding protein [FABP]-4) and mal1 (EFABP) are closely related and both are expressed in adipocytes. Absence of EFABP/mal1 resulted in increased systemic insulin sensitivity in two models of obesity and insulin resistance. Adipocytes isolated from mal1-deficient mice also exhibited enhanced insulin-stimulated glucose transport capacity. In contrast, mice expressing high levels of mal1 in adipose tissue display reduced systematic insulin activity.

    • Synonyms

      Fatty acid-binding protein epidermal, E-FABP, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, PA-FABP, FABP5, EFABP, PAFABP.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.

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

    Fabp5 Human His
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