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Name :
CCNB1 HumanDescription:
Cyclin-B1 Human Recombinant
G2/mitotic-specific cyclin-B1, cyclin B1, CCNB.
Product # :
PKA-037Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCNB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 457 amino acids (1-433) and having a molecular mass of 50.9 kDa.CCNB1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CCNB1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cyclin B1 (CCNB1) is a regulatory protein involved in mitosis. CCNB1 creates a complex with p34(cdc2) to form the maturation-promoting factor (MPF). CCNB1 is vital for the control of the cell cycle at the G2/M (mitosis) transition. CCNB1 builds up steadily during the G2 and is immediately destroyed at mitosis. The 2 alternative transcripts produce a constitutively expressed transcript and a cell cycle-regulated transcript which is expressed predominantly during G2/M phase. These transcripts are a result of alternate transcription initiation sites.
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Synonyms
G2/mitotic-specific cyclin-B1, cyclin B1, CCNB.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMALRVT RNSKINAENK AKINMAGAKR VPTAPAATSK PGLRPRTALG DIGNKVSEQL QAKMPMKKEA KPSATGKVID KKLPKPLEKV PMLVPVPVSE PVPEPEPEPE PEPVKEEKLS PEPILVDTAS PSPMETSGCA PAEEDLCQAF SDVILAVNDV DAEDGADPNL CSEYVKDIYA YLRQLEEEQA VRPKYLLGRE VTGNMRAILI DWLVQVQMKF RLLQETMYMT VSIIDRFMQN NCVPKKMLQL VGVTAMFIAS KYEEMYPPEI GDFAFVTDNT YTKHQIRQME MKILRALNFG LGRPLPLHFL RRASKIGEVD VEQHTLAKYL MELTMLDYDM VHFPPSQIAA GAFCLALKIL DNGEWTPTLQ HYLSYTEESL LPVMQHLAKN VVMVNQGLTK HMTVKNKYAT SKHAKISTLP QLNSALVQDL AKAVAKV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LAMTOR4 HumanDescription:
LAMTOR4 Human Recombinant
Late Endosomal/Lysosomal Adaptor, MAPK And MTOR Activator 4, C7orf59, Late Endosomal/Lysosomal Adaptor And MAPK And MTOR Activator 4, Chromosome 7 Open Reading Frame 59, Ragulator Complex Protein LAMTOR4, UPF0539 Protein C7orf59, LAMTOR4.
Product # :
PRO-2065Price :
Quantity :
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Shipped with Ice Packs
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Description
LAMTOR4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 122 amino acids (1-99 a.a) and having a molecular mass of 13.1kDa. LAMTOR4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAMTOR4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
LAMTOR4 is implicated in amino acid sensing and activation of mTORC1, which is a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. LAMTOR4 is activated by amino acids via a mechanism which involves the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases both function as a scaffold recruiting mTORC1 to lysosomes where it is sequentially activated.
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Synonyms
Late Endosomal/Lysosomal Adaptor, MAPK And MTOR Activator 4, C7orf59, Late Endosomal/Lysosomal Adaptor And MAPK And MTOR Activator 4, Chromosome 7 Open Reading Frame 59, Ragulator Complex Protein LAMTOR4, UPF0539 Protein C7orf59, LAMTOR4.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTSALTQ GLERIPDQLG YLVLSEGAVL ASSGDLENDE QAASAISELV STACGFRLHR GMNVPFKRLS VVFGEHTLLV TVSGQRVFVV KRQNRGREPI DV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ZMAT3 HumanDescription:
Zinc Finger, Matrin-Type 3 Human Recombinant
Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.
Product # :
PRO-1635Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ZMAT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 312 amino acids (1-289) and having a molecular mass of 34.4kDa.ZMAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ZMAT3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ZMAT3 is a protein with a nuclear localization signal and 3 zinc finger domains. The mRNA and the protein of this gene are upregulated by wildtype p53. When overexpressed, ZMAT3 can produce tumor cell growth, indicating that ZMAT3 takes part in the p53-dependent growth regulatory pathway. Alternative splicing of ZMAT3 produce two transcript variants encoding two isoforms differing in only one amino acid.
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Synonyms
Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMILLQHA VLPPPKQPSP SPPMSVATRS TGTLQLPPQK PFGQEASLPL AGEEELSKGG EQDCALEELC KPLYCKLCNV TLNSAQQAQA HYQGKNHGKK LRNYYAANSC PPPARMSNVV EPAATPVVPV PPQMGSFKPG GRVILATEND YCKLCDASFS SPAVAQAHYQ GKNHAKRLRL AEAQSNSFSE SSELGQRRAR KEGNEFKMMP NRRNMYTVQN NSAGPYFNPR SRQRIPRDLA MCVTPSGQFY CSMCNVGAGE EMEFRQHLES KQHKSKVSEQ RYRNEMENLG YV
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.
- View Data Sheet
Name :
SYT11 HumanDescription:
Synaptotagmin XI Human Recombinant
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
Product # :
PRO-2301Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SYT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (37-431 a.a) and having a molecular mass of 47kDa. SYT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SYT11 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 50% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.
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Synonyms
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSWSCCHQQ AEKKQKNPPY KFIHMLKGIS IYPETLSNKK KIIKVRRDKD GPGREGGRRN LLVDAAEAGL LSRDKDPRGP SSGSCIDQLP IKMDYGEELR SPITSLTPGE SKTTSPSSPE EDVMLGSLTF SVDYNFPKKA LVVTIQEAHG LPVMDDQTQG SDPYIKMTIL PDKRHRVKTR VLRKTLDPVF DETFTFYGIP YSQLQDLVLH FLVLSFDRFS RDDVIGEVMV PLAGVDPSTG KVQLTRDIIK RNIQKCISRG ELQVSLSYQP VAQRMTVVVL KARHLPKMDI TGLSGNPYVK VNVYYGRKRI AKKKTHVKKC TLNPIFNESF IYDIPTDLLP DISIEFLVID FDRTTKNEVV GRLILGAHSV TASGAEHWRE VCESPRKPVA KWHSLSEY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NCL HumanDescription:
Nucleolin Human Recombinant
Nucleolin, Protein C23, NCL, C23.
Product # :
PRO-1508Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.
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Synonyms
Nucleolin, Protein C23, NCL, C23.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Name :
TGFB3 RatDescription:
Transforming Growth Factor-Beta 3 Rat Recombinant
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Product # :
CYT-1269Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFB3 Rat Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.
Purity
Greater than 97.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.More Info
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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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.
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Solubility
It is recommended to reconstitute the lyophilized TGFB3 in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSSDTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
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Background
Recombinant TGF-β3 Rat is commonly used in cell culture and biomedical research to investigate TGF-β signalling, stem cell differentiation, tissue engineering, chondrogenesis, wound healing, fibrosis, and cancer biology. TGFB3 is added to mesenchymal stem cell and chondrocyte cultures to promote cartilage formation and maintain specific cellular phenotypes under defined experimental conditions.
What is the molecular weight / Mw of TGFB3 Rat Protein?
TGFB3 Rat Protein has a total Mw of 25kDa.
What is the source or expression system of TGFB3 Rat Protein?
CHO Cells
What is the Purity of TGFB3 Rat Protein?
TGFB3 rat Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of TGFB3 rat Protein?
Determined by the ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0×107 units/mg.
What is the amino acid sequence of TGFB3 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS
What applications can TGFB3 rat Protein be used in?
TGFB3 rat Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TGFB3 rat Protein?
The endotoxin level is minimal, TGFB3 rat 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.
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Name :
ACVR1 HumanDescription:
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-1140Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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
More Info
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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.
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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.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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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.
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Name :
Leptin tA HumanDescription:
Leptin Antagonist Triple Mutant Human Recombinant
Product # :
CYT-352Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LIF HumanDescription:
Leukemia Inhibitory Factor Human Recombinant
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-644Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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.
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Solubility
It is recommended to reconstitute the lyophilized Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
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Background
Leukemia Inhibitory Factor (LIF) Background
Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.
LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.
Function and Applications of LIF
LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.
Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.
Structure and Interactions
LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CTLA4 Human, igG-HisDescription:
Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant, igG-His Tag
CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.
Product # :
CYT-985Price :
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Description
CTLA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 368 amino acids (36-161a.a.) and having a molecular mass of 40.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTLA4 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTLA4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.
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Synonyms
CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.
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Background
What is the molecular weight/Mw of CTLA4 Protein?
CTLA4 Protein has a total Mw of 40.8kDa.
What is the source or expression system of CTLA4 Protein?
Sf9, Baculovirus cells.
What is the Purity of CTLA4 Protein?
CTLA4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTLA4 Protein?
The biological functionality of CTLA4 Protein will be determined in the future.
What is the amino acid sequence of CTLA4 Protein?
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.
What applications can CTLA4 Protein be used in?
CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTLA4 Protein?
The endotoxin level is minimal, CTLA4 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.
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Name :
STOM HumanDescription:
Stomatin Human Recombinant
BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.
Product # :
PRO-1525Price :
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Description
STOM Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (55-288) and having a molecular mass of 28 kDa. STOM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The STOM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Stomatin (STOM) is a part of a highly conserved family of integral membrane proteins. STOM is a membrane protein involved in regulation of monovalent cation transport through lipid membranes which regulates ACCN1 and ACCN3 gating. STOM is a major lipid-raft component of erythrocytes and epithelial cells, and an abundant platelet protein which acts as a cytoskeletal anchor.
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Synonyms
BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKIIKEYE RAIIFRLGRI LQGGAKGPGL FFILPCTDSF IKVDMRTISF DIPPQEILTK DSVTISVDGV VYYRVQNATL AVANITNADS ATRLLAQTTL RNVLGTKNLS QILSDREEIA HNMQSTLDDA TDAWGIKVER VEIKDVKLPV QLQRAMAAEA EASREARAKV IAAEGEMNAS RALKEASMVI TESPAALQLR YLQTLTTIAA EKNSTIVFPL PIDMLQGIIG AKHSHLG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RPS7 HumanDescription:
Ribosomal Protein S7 Human Recombinant
Ribosomal protein S7, DBA8, S7, 40S ribosomal protein S7.
Product # :
PRO-993Price :
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Description
RPS7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-194 a.a.) and having a molecular mass of 24.7kDa.RPS7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RPS7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
RPS7 is a member of the S3P family of ribosomal proteins and is situated in the cytoplasm. RPS7 takes part in ribosomal stress, connecting ribosome biogenesis to cell death or cell cycle arrest. In addition, RPS7 cooperates with MDM2 and negatively regulate the MDM2-mediated degradation of p53.
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Synonyms
Ribosomal protein S7, DBA8, S7, 40S ribosomal protein S7.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMFSSSA KIVKPNGEKP DEFESGISQA LLELEMNSDL KAQLRELNIT AAKEIEVGGG RKAIIIFVPV PQLKSFQKIQ VRLVRELEKK FSGKHVVFIA QRRILPKPTR KSRTKNKQKR PRSRTLTAVH DAILEDLVFP SEIVGKRIRV KLDGSRLIKV HLDKAQQNNV EHKVETFSGV YKKLTGKDVN FEFPEFQL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SOST HumanDescription:
Sclerostin Human Recombinant
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-1601Price :
Quantity :
Shipping Method :
Shipped at Room temp
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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
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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.
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Synonyms
Sclerostin, SOST, CDD, VBCH.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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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.
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Name :
BTLA HumanDescription:
B And T Lymphocyte Associated Human Recombinant
B- and T-lymphocyte attenuator, B- and T-lymphocyte-associated protein, CD272, B And T Lymphocyte Associated, B- And T-Lymphocyte-Associated Protein, B- And T, Lymphocyte Attenuator, CD272 Antigen, BTLA1.
Product # :
PRO-2505Price :
Quantity :
Shipping Method :
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Description
BTLA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 136 amino acids (31-157 a.a.) and having a molecular mass of 15.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).BTLA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
BTLA protein 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
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Introduction
BTLA, also known as B And T Lymphocyte Associated, is an inhibitory molecule which is part of the Ig superfamily. BTLA is a type 1 transmembrane glycoprotein in the CD28 family of T cell costimulatory molecules. BTLA is a 3rd inhibitory receptor on T lymphocytes with resemblances to CTLA-4 & PD-1. Moreover, BTLA is a ligand for TNF (receptor) superfamily, TNFRSF14, and HVEM. BTLA-HVEM complexes negatively regulate T-cell immune responses.
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Synonyms
B- and T-lymphocyte attenuator, B- and T-lymphocyte-associated protein, CD272, B And T Lymphocyte Associated, B- And T-Lymphocyte-Associated Protein, B- And T, Lymphocyte Attenuator, CD272 Antigen, BTLA1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
ADPKESCDVQ LYIKRQSEHS ILAGDPFELE CPVKYCANRP HVTWCKLNGT TCVKLEDRQT SWKEEKNISF FILHFEPVLP NDNGSYRCSA NFQSNLIESH STTLYVTDVK SASERPSKDE MASRPWLLYS HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TUBG1 Human, Sf9Description:
Tubulin Gamma 1 Human Recombinant, Sf9
Tubulin gamma-1 chain, Gamma-1-tubulin, Gamma-tubulin complex component 1, GCP-1, TUBG1, TUBG, Tubulin, Gamma 1, Gamma-1-Tubulin, TUBGCP1, CDCBM4.
Product # :
PRO-2532Price :
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Description
TUBG1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 457 amino acids (1-451 a.a.) and having a molecular mass of 51.9kDa. TUBG1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
TUBG1 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 8.0) containing 40% glycerol, 0.1M NaCl,2mM DTT and 50mM imidazole.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TUBG1 belongs to the tubulin superfamily. TUBG1 localizes to the centrosome and binds to microtubules to create the gamma-tubulin ring complex. TUBG1 facilitates the microtubule nucleation and is essential for microtubule formation and progression of the cell cycle.
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Synonyms
Tubulin gamma-1 chain, Gamma-1-tubulin, Gamma-tubulin complex component 1, GCP-1, TUBG1, TUBG, Tubulin, Gamma 1, Gamma-1-Tubulin, TUBGCP1, CDCBM4.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE QHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LIFR MouseDescription:
Leukemia Inhibitory Factor Receptor Alpha Mouse Recombinant
Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.
Product # :
CYT-1170Price :
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Description
LIFR Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 794 amino acids (44-828 aa) and having a molecular mass of 89.6kDa.LIFR is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LIFR protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit proliferation using TF-1 human erythroleukemic cells. The ED50 range ≤ 1ug/ml with Mouse LIF.
More Info
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Introduction
Leukemia Inhibitory Factor Receptor Alpha or LIFR is a protein, part of the Interleukin-6 receptor group of proteins. As such, LIFR acts as a mediator for various proteins (IL-6, IL-11, IL-27, Oncostatin M etc). LIFR has many functions as a cytokine, he has an affect on the cell proliferation, differentiation and survival in the different stages of life. In different types of breast cancer LIFR is down regulated, and as such, can be used as a prognostic tool.
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Synonyms
Leukemia inhibitory factor receptor, LIF receptor, LIF-R, D-factor/LIF receptor, CD118, CD antigen, leukemia inhibitory factor receptor isoform 1 precursor, Lifr.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPLKRGVQD LKCTTNNMRV WDCTWPAPLG VSPGTVKDIC IKDRFHSCHP LETTNVKIPA LSPGDHEVTI NYLNGFQSKF TLNEKDVSLI PETPEILDLS ADFFTSSLLL KWNDRGSALP HPSNATWEIK VLQNPRTEPV ALVLLNTMLS GKDTVQHWNW TSDLPLQCAT HSVSIRWHID SPHFSGYKEW SDWSPLKNIS WIRNTETNVF PQDKVVLAGS NMTICCMSPT KVLSGQIGNT LRPLIHLYGQ TVAIHILNIP VSENSGTNII FITDDDVYGT VVFAGYPPDV PQKLSCETHD LKEIICSWNP GRITGLVGPR NTEYTLFESI SGKSAVFHRI EGLTNETYRL GVQMHPGQEI HNFTLTGRNP LGQAQSAVVI NVTERVAPHD PTSLKVKDIN STVVTFSWYL PGNFTKINLL CQIEICKANS KKEVRNATIR GAEDSTYHVA VDKLNPYTAY TFRVRCSSKT FWKWSRWSDE KRHLTTEATP SKGPDTWREW SSDGKNLIVY WKPLPINEAN GKILSYNVSC SLNEETQSVL EIFDPQHRAE IQLSKNDYII SVVARNSAGS SPPSKIASME IPNDDITVEQ AVGLGNRIFL TWRHDPNMTC DYVIKWCNSS RSEPCLLDWR KVPSNSTETV IESDQFQPGV RYNFYLYGCT NQGYQLLRSI IGYVEELAPI VAPNFTVEDT SADSILVKWD DIPVEELRGF LRGYLFYFQK GERDTPKTRS LEPHHSDIKL KNITDISQKT LRIADLQGKT SYHLVLRAYT HGGLGPEKSM FVVTKENSHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LILRB1 HumanDescription:
Leukocyte Immunoglobulin Like Receptor B1 Human Recombinant
Leukocyte immunoglobulin-like receptor subfamily B member 1,Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B
Product # :
PRO-2668Price :
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Description
LILRB1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (24-461 a.a) and having a molecular mass of 48.5kDa.LILRB1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The LILRB1 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Biological activity is > 50%. It is defined by the ability of the immobilized protein to support the adhesion of HSB2 human peripheral blood acute lymphoblastic leukemia cells, while the cells are added to LILRB1 coated plates at 5ug/ml.
More Info
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Introduction
Leukocyte Immunoglobulin Like Receptor B1 (LILRB1) is a member of the leukocyteimmunoglobulinlike receptor (LIR) family. LILRB1is expressed on immune cells, binds to MHC classI molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immuneresponse. LILRB1 controls inflammatory responses and cytotoxicity to help focus the immune responseand limit autoreactivity. LILRB1 is also expressed on the surface of B cells and monocytes, subsets of NKcells, gamma δ T cells,memory/effector CD8+ T cells and monocyte-derived dendritic cells.
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Synonyms
Leukocyte immunoglobulin-like receptor subfamily B member 1,
Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B -
Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
GHLPKPTLWA EPGSVITQGS PVTLRCQGGQ ETQEYRLYRE KKTAPWITRI PQELVKKGQF PIPSITWEHT GRYRCYYGSD TAGRSESSDP LELVVTGAYI KPTLSAQPSP VVNSGGNVTL QCDSQVAFDG FILCKEGEDE HPQCLNSQPH ARGSSRAIFS VGPVSPSRRW WYRCYAYDSN SPYEWSLPSD LLELLVLGVS KKPSLSVQPG PIVAPEETLT LQCGSDAGYN RFVLYKDGER DFLQLAGAQP QAGLSQANFT LGPVSRSYGG QYRCYGAHNL SSEWSAPSDP LDILIAGQFY DRVSLSVQPG PTVASGENVT LLCQSQGWMQ TFLLTKEGAA DDPWRLRSTY QSQKYQAEFP MGPVTSAHAG TYRCYGSQSS KPYLLTHPSD PLELVVSGPS GGPSSPTTGP TSTSGPEDQP LTPTGSDPQS GLGRHLGVLE HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LILRB2 HumanDescription:
Leukocyte Immunoglobulin Like Receptor B2 Human Recombinant
Leukocyte Immunoglobulin-like Receptor, CD85D, CD85d, CD85 antigen-like family member D, CD85d antigen, ILT-4, ILT4, ILT4CD85d, Ig-like transcript 4, Immunoglobulin-like transcript 4, LILRB2, LIR2, LIR-2, LIR2CD85D, Leukocyte immunoglobulin-like receptor 2, MIR10, MIR-10, MIR10LILRA6, Monocyte/macrophage immunoglobulinlike receptor 10, leukocyte immunoglobulin-like receptor subfamily B member 2, leukocyte immunoglobulin-like receptor subfamily B member 2 soluble isoform 1.
Product # :
PRO-2729Price :
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Description
LILRB2 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 444 amino acids (24-461 a.a) and having a molecular mass of 48.3kDa.LILRB2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The LILRB2 solution (0. 5mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Leukocyte Immunoglobulin Like Receptor B2 (LILRB2) is a member of the leukocyte immunoglobulin-like receptor (LIR) family. LILRB2is expressed on immune cells where it binds to MHC class I molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immune response.LILRB2controls inflammatory responses and cytotoxicity to help focus the immune response and limit autoreactivity.LILRB2competes with CD8 alpha for MHC I binding. LILRB2binds to classical MHC I proteins as well as the non-classical HLA-G1 and HLA-F molecules.
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Synonyms
Leukocyte Immunoglobulin-like Receptor, CD85D, CD85d, CD85 antigen-like family member D, CD85d antigen, ILT-4, ILT4, ILT4CD85d, Ig-like transcript 4, Immunoglobulin-like transcript 4, LILRB2, LIR2, LIR-2, LIR2CD85D, Leukocyte immunoglobulin-like receptor 2, MIR10, MIR-10, MIR10LILRA6, Monocyte/macrophage immunoglobulinlike receptor 10, leukocyte immunoglobulin-like receptor subfamily B member 2, leukocyte immunoglobulin-like receptor subfamily B member 2 soluble isoform 1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
GTIPKPTLWA EPDSVITQGS PVTLSCQGSL EAQEYRLYRE KKSASWITRI RPELVKNGQF HIPSITWEHT GRYGCQYYSR ARWSELSDPL VLVMTGAYPK PTLSAQPSPV VTSGGRVTLQ CESQVAFGGF ILCKEGEDEH PQCLNSQPHA RGSSRAIFSV GPVSPNRRWS HRCYGYDLNS PYVWSSPSDL LELLVPGVSK KPSLSVQPGP VMAPGESLTL QCVSDVGYDR FVLYKEGERD LRQLPGRQPQ AGLSQANFTL GPVSRSYGGQ YRCYGAHNLS SECSAPSDPL DILITGQIRG TPFISVQPGP TVASGENVTL LCQSWRQFHT FLLTKAGAAD APLRLRSIHE YPKYQAEFPM SPVTSAHAGT YRCYGSLNSD PYLLSHPSEP LELVVSGPSM GSSPPPTGPI STPAGPEDQP LTPTGSDPQS GLGRHLGVHH 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.
- View Data Sheet
Name :
MAGEA5 HumanDescription:
Melanoma Antigen Family A, 5 Human Recombinant
Melanoma antigen family A 5, Cancer/testis antigen 1.5, CT1.5, cancer/testis antigen family 1 member 5, MAGE-5 (5a/5b) antigen, MAGEA4, MGC129526.
Product # :
PRO-1070Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MAGEA5 Human Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (1-124) and having a molecular mass of 15.6kDa.MAGEA5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MAGEA5 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
MAGEA5 belongs to the MAGEA gene family which encodes proteins with 50 to 80% sequence identity to each other. The promoters and first exons of the MAGEA genes are variable, which signify that the presence of this gene family enables the same role to be expressed under diverse transcriptional controls. The MAGEA genes are clustered at chromosomal location Xq28. They are associated with several hereditary disorders, like dyskeratosis congenita. MAGEA5 gene encodes a protein which is C-terminally truncated compared to other family members, and can be alternatively interpreted to be a pseudogene.
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Synonyms
Melanoma antigen family A 5, Cancer/testis antigen 1.5, CT1.5, cancer/testis antigen family 1 member 5, MAGE-5 (5a/5b) antigen, MAGEA4, MGC129526.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSLEQK SQHCKPEEGL DTQEEALGLV GVQAATTEEQ EAVSSSSPLV PGTLGEVPAA GSPGPLKSPQ GASAIPTAID FTLWRQSIKG SSNQEEEGPS TSPDPESVFR AALSKKVADL IHFLLLKY
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.
- View Data Sheet
Name :
VEGF Mouse, Sf9Description:
Vascular Endothelial Growth Factor Mouse Recombinant, Sf9
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-226Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Vascular Endothelial Growth Factor Mouse Recombinant produced in Sf9 insect cells is a double, glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 48 kDa.The VEGF is purified by proprietary chromatographic techniques.
Source
Baculovirus Sf9 cells.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 range, determined by the dose-dependent proliferation of human umbilical vein endothelial cells (HUVEC) (measured by 3H-thymidine uptake) is 1-2 ng/ml, corresponding to a specific activity of 1x106 Units/mg.More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vascular Endothelial Growth Factor Sf9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-Sf9 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.
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Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor-Sf9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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.
- View Data Sheet
Name :
MAPT Human 381a.a.Description:
Microtubule-Associated Protein Tau 381 a.a. Human Recombinant
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Product # :
PRO-042Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MAPT Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 41.8kDa. The NCBI Accession No. is EAW93573.1.The MAPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT and 20% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Microtubule-associated protein tau (MAPT or Tau) is a protein that stabilizes microtubules. MAPT is abundant in neurons in the central nervous system and is less common elsewhere. When MAPT is defective, and no longer stabilizes microtubules properly, it can result in dementias, such as Alzheimer's disease.
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Synonyms
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIVY
KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RCN1 HumanDescription:
Reticulocalbin 1 Human Recombinant
PIG20, RCAL, RCN.
Product # :
PRO-544Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RCN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (30-331 a.a.) and having a molecular mass of 40.4kDa (real molecular weight on SDS-PAGE will be shift up). The RCN1 is fused to 39 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
RCN1 is a calcium-binding protein which binds calcium and controls calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. RCN1 withholds six conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.
High conservation of amino acid residues outside of these motifs, in relation to mouse reticulocalbin, is consistent with a biochemical function further to that of calcium binding. In human endothelial and prostate cancer cell lines RCN1 protein is localized to the plasma membrane. -
Synonyms
PIG20, RCAL, RCN.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEK PTVRKERVVR PDSELGERPP EDNQSFQYDH EAFLGKEDSK TFDQLTPDES
KERLGKIVDR IDNDGDGFVT TEELKTWIKR VQKRYIFDNV AKVWKDYDRD KDDKISWEEY KQATYGYYLG NPAEFHDSSD HHTFKKMLPR
DERRFKAADL NGDLTATREE FTAFLHPEEF EHMKEIVVLE TLEDIDKNGD GFVDQDEYIA DMFSHEENGP EPDWVLSERE QFNEFRDLNK
DGKLDKDEIR HWILPQDYDH AQAEARHLVY ESDKNKDEKL TKEEILENWN MFVGSQATNY GEDLTKNHDE L.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RRM2 HumanDescription:
Ribonucleotide Reductase M2 Human Recombinant
EC 1.17.4.1, RR2M, RR2, Ribonucleotide Reductase M2, R2, RRM2.
Product # :
ENZ-523Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RRM2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-389 a.a.) and having a molecular mass of 47 kDa. The RRM2 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RRM2 protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis RRM2 is regulated in a cell-cycle dependent method. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RRM2 Inhibits Wnt signaling.
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Synonyms
EC 1.17.4.1, RR2M, RR2, Ribonucleotide Reductase M2, R2, RRM2.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLSLRVPLAP ITDPQQLQLS PLKGLSLVDK ENTPPALSGT RVLASKTARR IFQEPTEPKT KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS FWTAEEVDLS KDIQHWESLK PEERYFISHV LAFFAASDGI VNENLVERFS QEVQITEARC FYGFQIAMEN IHSEMYSLLI DTYIKDPKER EFLFNAIETM PCVKKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF ASIFWLKKRG LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRIE QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM ENISLEGKTN FFEKRVGEYQ RMGVMSSPTE NSFTLDADF.
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.
- View Data Sheet
Name :
MIS12 HumanDescription:
MIS12 Human Recombinant
hMis12, KNTC2AP, MTW1, Protein MIS12 homolog.
Product # :
PRO-022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MIS12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-205 a.a.) and having a molecular mass of 26.5kDa. MIS12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIS12 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0) ,2M Urea and10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein MIS12 Belongs to the mis12 family. MIS12 is an element of the MIS12 complex, which is necessary for kinetochore formation during mitosis and normal chromosome alignment and segregation. The MIS12 complex which comprised of MIS12,DSN1 , NSL1 and PMF-1. MIS12 is section of a network of complexes that supply microtubule attachment and generates pulling forces from depolymerization.
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Synonyms
hMis12, KNTC2AP, MTW1, Protein MIS12 homolog.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSVDPMT YEAQFFGFTP QTCMLRIYIA FQDYLFEVMQ AVEQVILKKL DGIPDCDISP VQIRKCTEKF LCFMKGHFDN LFSKMEQLFL QLILRIPSNI LLPEDKCKET PYSEEDFQHL QKEIEQLQEK YKTELCTKQA LLAELEEQKI VQAKLKQTLT FFDELHNVGR DHGTSDFRES LVSLVQNSRK LQNIRDNVEK ESKRLKIS.
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.