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1000 results found for “Cofilin”
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Name :
KPNB1 HumanDescription:
Karyopherin Beta 1 Human Recombinant
Importin subunit beta-1, Importin-90, Karyopherin subunit beta-1, Nuclear factor p97, Pore targeting complex 97kDa subunit, PTAC97, KPNB1, NTF97.
Product # :
PRO-1001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KPNB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 899 amino acids (1-876 a.a.) and having a molecular mass of 99.6kDa. KPNB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
KPNB1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
KPNB1 is a member of the importin beta family. The KPNB1 protein is engaged in nuclear protein import, either by coupling itself with an adapter protein (e.g., importin-alpha subunit which binds to nuclear localization signals (NLS) in cargo substrates), or by functioning autonomously as a nuclear transport receptor (acts as NLS receptor, docking of the importin/substrate complex to the nuclear pore complex).
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Synonyms
Importin subunit beta-1, Importin-90, Karyopherin subunit beta-1, Nuclear factor p97, Pore targeting complex 97kDa subunit, PTAC97, KPNB1, NTF97.
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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 MGSMELITIL EKTVSPDRLE LEAAQKFLER AAVENLPTFL VELSRVLANP GNSQVARVAA GLQIKNSLTS KDPDIKAQYQ QRWLAIDANA RREVKNYVLQ TLGTETYRPS SASQCVAGIA CAEIPVNQWP ELIPQLVANV TNPNSTEHMK ESTLEAIGYI CQDIDPEQLQ DKSNEILTAI IQGMRKEEPS NNVKLAATNA LLNSLEFTKA NFDKESERHF IMQVVCEATQ CPDTRVRVAA LQNLVKIMSL YYQYMETYMG PALFAITIEA MKSDIDEVAL QGIEFWSNVC DEEMDLAIEA SEAAEQGRPP EHTSKFYAKG ALQYLVPILT QTLTKQDEND DDDDWNPCKA AGVCLMLLAT CCEDDIVPHV LPFIKEHIKN PDWRYRDAAV MAFGCILEGP EPSQLKPLVI QAMPTLIELM KDPSVVVRDT AAWTVGRICE LLPEAAINDV YLAPLLQCLI EGLSAEPRVA SNVCWAFSSL AEAAYEAADV ADDQEEPATY CLSSSFELIV QKLLETTDRP DGHQNNLRSS AYESLMEIVK NSAKDCYPAV QKTTLVIMER LQQVLQMESH IQSTSDRIQF NDLQSLLCAT LQNVLRKVQH QDALQISDVV MASLLRMFQS TAGSGGVQED ALMAVSTLVE VLGGEFLKYM EAFKPFLGIG LKNYAEYQVC LAAVGLVGDL CRALQSNIIP FCDEVMQLLL ENLGNENVHR SVKPQILSVF GDIALAIGGE FKKYLEVVLN TLQQASQAQV DKSDYDMVDY LNELRESCLE AYTGIVQGLK GDQENVHPDV MLVQPRVEFI LSFIDHIAGD EDHTDGVVAC AAGLIGDLCT AFGKDVLKLV EARPMIHELL TEGRRSKTNK AKTLATWATK ELRKLKNQA.
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 :
GIP HumanDescription:
Gastric Inhibitory Polypeptide Human Recombinant
Gastric inhibitory polypeptide, GIP, Incretin hormone.
Product # :
PRO-1438Price :
Quantity :
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Shipped with Ice Packs
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Description
GIP Human Recombinant produced in E. coli is a single polypeptide chain containing 155 amino acids (22-153) and having a molecular mass of 17.3kDa. GIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GIP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol 0.1M NaCl and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Gastric Inhibitory Polypeptide (GIP) which is a significant hormone of the enteroinsular axis has a functional profile of possible therapeutic value for type 2 diabetes. GIP is an important incretin hormone released into the circulation from endocrine K-cells of the duodenum and jejunum after ingestion of food1. GIP was evaluated for his ability to elevate cellular cAMP production. GIP promotes plasma triglyceride clearance in response to oral fat loading.
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Synonyms
Gastric inhibitory polypeptide, GIP, Incretin hormone.
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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 MGSEKKEGHF SALPSLPVGS HAKVSSPQPR GPRYAEGTFI SDYSIAMDKI HQQDFVNWLL AQKGKKNDWK HNITQREARA LELAGQANRK EEEAVEPQSS PAKNPSDEDL LRDLLIQELL ACLLDQTNLC RLRSR.
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 :
M CSF RatDescription:
Macrophage-Colony Stimulating Factor Rat Recombinant
Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.
Product # :
CYT-856Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Colony Stimulating Factor Rat Recombinant produced in E.coli is a non-glycosylated homodimer, containing 2 x 155 amino acids and having a total molecular mass of 36.2 kDa.MCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile filtered aqueous solution containing 10mM Na3PO4, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity as determined by dose-dependent induction of M-NFS-60 cell proliferation is 1.65 ng/ml. This corresponds to an expected specific activity of 6.1x105 units/mg.
More Info
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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
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Synonyms
Macrophage colony-stimulating factor 1, CSF-1, MCSF, Csf1, Csfm.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MEVSEHCSHM IGNGHLQILQ QLIDSQMETA CLIEYKFVDQ EQLDDPVCYL KKAFVLVQVI IEETMRFKDN TPNANATERL QELSMKLNSC FIKDYKEQNE ACVQTYKESP LRLLEKIKNF FNETKNFLEK DWNIFSKNCN DSLAKCSSRD VVTKP.
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 :
Resistin Human, HEKDescription:
Resistin Human Recombinant, HEK
RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.
Product # :
CYT-1183Price :
Quantity :
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Shipped with Ice Packs
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Description
Resistin Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (19-108 a.a) containing 96 amino acids and having a molecular mass of 10.3 kDa.Resistin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
Resistin protein (1mg/ml) contains 20% glycerol and 20mM Sodium citrate (pH3.0).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis.Resistin blocks insulinstimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of lowdensity lipoprotein (LDL), increasing the risk of heart disease.
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Synonyms
RETN,ADSF,FIZZ3,RETN1,RSTN,XCP1,resistin precursor, Adipose tissue-specific secretory factor, ADSFMGC126609, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, Cysteine-rich secreted protein FIZZ3, FIZZ3; FIZZ3MGC126603, found in inflammatory zone 3, HXCP1.
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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
KTLCSMEEAI NERIQEVAGS LIFRAISSIG LECQSVTSRG DLATCPRGFA VTGCTCGSAC GSWDVRAETT CHCQCAGMDW TGARCCRVQP 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 :
CoV-2 N (196 a.a.)Description:
Coronavirus 2019 Nucleocapsid (196 a.a.), Recombinant
Product # :
SARS-042Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the Coronavirus 2019 middle region a.a. from the Nucleocapsid protein and fused to GST-6xHis tag at N-terminal and having a Mw. Of 48.4 kDa.
Source
E.Coli.
Formulation
CoV-2 Nucleocapsid protein solution is supplied in 50mM Tris-HCl pH 8, 1M Urea, and 50% Glycerol.
Purity
CoV-2 Nucleocapsid protein is >95% pure as determined SDS-PAGE.
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CoV-2 Spike Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Purification Method
NTA Sepharose-Affinity Purification.
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 :
ZNF32 HumanDescription:
Zinc Finger Protein 32 Human Recombinant
KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.
Product # :
PRO-1983Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ZNF32 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a) and having a molecular mass of 33.4kDa. ZNF32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNF32 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Finger Protein 32 (ZNF32) is a part of the krueppel C2H2-type zinc-finger protein family. ZNF32 which contains seven C2H2-type zinc fingers takes part in transcriptional regulation.
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Synonyms
KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.
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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 MGSMFGFPTA TLLDCHGRYA QNVAFFNVMT EAHHKYDHSE ATGSSSWDIQ NSFRREKLEQ KSPDSKTLQE DSPGVRQRVY ECQECGKSFR QKGSLTLHER IHTGQKPFEC THCGKSFRAK GNLVTHQRIH TGEKPYQCKE CGKSFSQRGS LAVHERLHTG QKPYECAICQ RSFRNQSNLA VHRRVHSGEK PYRCDQCGKA FSQKGSLIVH IRVHTGLKPY ACTQCRKSFH TRGNCILHGK IHTGETPYLC GQCGKSFTQR GSLAVHQRSC SQRLTL.
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 :
SAR1A HumanDescription:
GTP-Binding Protein SAR1A Human Recombinant
GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.
Product # :
PRO-709Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SAR1A Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids (1- 198 a.a.) and having a molecular mass of 24.5kDa.The SAR1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SAR1A solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SAR1A is a member of the small GTPase superfamily. SAR1A is a vital component of COPII vesicle coats involved in export of cargo from the ER (Endoplasmic Reticulum). The GTPase activity of SAR1A serves as a molecular switch to control protein-protein and protein-lipid interactions which dictate vesicle budding from the ER. SAR1A, while GDP-bound interacts with the membrane-bound exchange factor Sec12 and trades its bound GDP for GTP. SAR1A is also involved in the transport from the ER to the Golgi apparatus. SAR1A is required to maintain SEC16A localization at distinct locations on the ER membrane possibly by preventing its dissociation. SAR1A-GTP-dependent compilation of SEC16A on the ER membrane creates a structured scaffold defining endoplasmic reticulum exit sites.
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Synonyms
GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.
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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 MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLVE SKVELNALMT DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV LKRQGYGEGF RWLSQYID.
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 :
CXADR HumanDescription:
Coxsackie Virus And Adenovirus Receptor Human Recombinant
Coxsackie Virus And Adenovirus Receptor, CAR, 46 KD Coxsackievirus And Adenovirus Receptor (CAR) Protein 11, Coxsackievirus B-Adenovirus Receptor, HCVADR, CVB3-Binding Protein, CAR4/6, HCAR.
Product # :
PRO-1548Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CXADR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (20-237) and having a molecular mass of 26.0kDa.CXADR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXADR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CXADR is a component of the epithelial apical junction complex which operates as an homophilic cell adhesion molecule and is crucial for tight junction integrity. CXADR also takes part in transepithelial relocation of leukocytes through adhesive interactions with AMICA1/JAML a transmembrane protein of the plasma membrane of leukocytes. A number of transcript variants encoding different isoforms were identified for this gene. Pseudogenes of this gene were located on chromosomes 15, 18, and 21.
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Synonyms
Coxsackie Virus And Adenovirus Receptor, CAR, 46 KD Coxsackievirus And Adenovirus Receptor (CAR) Protein 11, Coxsackievirus B-Adenovirus Receptor, HCVADR, CVB3-Binding Protein, CAR4/6, HCAR.
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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 MGSLSITTPE EMIEKAKGET AYLPCKFTLS PEDQGPLDIE WLISPADNQK VDQVIILYSG DKIYDDYYPD LKGRVHFTSN DLKSGDASIN VTNLQLSDIG TYQCKVKKAP GVANKKIHLV VLVKPSGARC YVDGSEEIGS DFKIKCEPKE GSLPLQYEWQ KLSDSQKMPT SWLAEMTSSV ISVKNASSEY SGTYSCTVRN RVGSDQCLLR LNVVPPSNKA G.
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 :
AITRL HumanDescription:
AITRL Human Recombinant
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
Product # :
CYT-076Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AITRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (72-199) and having a molecular mass of 14.6 kDa.AITRL is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AITRL solution (0.5mg/ml) contains 10mM sodium citrate (pH 3.5), 1mMDTT and 10% glycerol
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Synonyms
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
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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
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LLANPQFIS
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Background
AITRL Human Recombinant: Unraveling its Significance in Immune Modulation and Therapeutic Implications
1. Abstract
This research paper provides a comprehensive examination of AITRL Human Recombinant, an essential protein involved in immune modulation. By exploring its structure, signaling mechanisms, biological functions, and implications in disease pathology, we shed light on the potential therapeutic applications of AITRL in immune-related disorders.
2. Introduction
AITRL, also known as TNFSF18, is a receptor protein belonging to the tumor necrosis factor superfamily. It plays a crucial role in immune regulation and has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.
3. Structure and Signaling of AITRL
AITRL is a transmembrane protein with a conserved TNF domain. It interacts with its receptor, AITR (TNFRSF18), leading to downstream signaling events that modulate immune cell function. The binding of AITRL to AITR promotes immune cell activation and cytokine production.
4. Biological Functions of AITRL
AITRL is involved in the regulation of immune responses by influencing T-cell activation, proliferation, and differentiation. It can stimulate effector T-cell responses while also promoting the development and function of regulatory T cells, thus maintaining immune homeostasis.
5. AITRL in Disease Pathology
Dysregulation of AITRL signaling has been implicated in various immune-related disorders, including autoimmune diseases, allergic reactions, and cancer. AITRL's involvement in disease pathology highlights its significance as a potential therapeutic target.
6. Therapeutic Potential of AITRL
The unique role of AITRL in immune modulation presents opportunities for therapeutic interventions. Modulating AITRL signaling holds promise for manipulating immune responses in the context of autoimmune diseases, allergic disorders, and cancer immunotherapy.
7. Conclusion and Future Perspectives
While our understanding of AITRL and its functions has advanced significantly, further research is needed to unravel its complex signaling pathways and therapeutic potential fully. Continued investigations into AITRL biology will pave the way for the development of targeted therapies for immune-related disorders.
What is the molecular weight/Mw of AITRL Protein?
AITRL Protein has a total Mw of 15.6kDa.
What is the source or expression system of AITRL Protein?
Escherichia Coli.
What is the Purity of AITRL Protein?
AITRL Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of AITRL Protein?
The biological functionality of AITRL Protein will be determined in the future.
What is the amino acid sequence of AITRL Protein?
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.
What applications can AITRL Protein be used in?
AITRL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AITRL Protein?
The endotoxin level is minimal, AITRL 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 :
DEFB118 HumanDescription:
Beta Defensin 118 Human Recombinant
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
Product # :
CYT-714Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.
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Synonyms
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
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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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
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Background
Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications
Abstract:
Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.Role in Innate Immunity:
BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.Therapeutic Implications:
Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.Conclusion:
Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.What is the molecular weight/Mw of DEFB118 Protein?
DEFB118 Protein has a total Mw of 13.8kDa.
What is the source or expression system of DEFB118 Protein?
Escherichia Coli.
What is the Purity of DEFB118 Protein?
DEFB118 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB118 Protein?
The biological functionality of DEFB118 Protein will be determined in the future.
What is the amino acid sequence of DEFB118 Protein?
MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
What applications can DEFB118 Protein be used in?
DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB118 Protein?
The endotoxin level is minimal, DEFB118 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.
- View Data Sheet
Name :
SNAPIN HumanDescription:
SNAP Associated Protein Human Recombinant
SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.
Product # :
PRO-663Price :
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Description
SNAPIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-136) and having a molecular mass of 17 kDa. SNAPIN is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl pH-8, 5mM DTT, 2mM EDTA, 0.2M NaCl, and 40% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.
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Synonyms
SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.
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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 MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINEDQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK.
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 :
EDF1 HumanDescription:
Endothelial Differentiation-Related Factor 1 Human Recombinant
EDF-1, MBF1, Multiprotein-bridging factor 1.
Product # :
PRO-494Price :
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Description
EDF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-148 a.a.) and having a molecular mass of 17.4 kDa. The EDF1 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5 mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
EDF1 controls endothelial cell differentiation. EDF1 has a role as a bridging protein that interconnects regulatory proteins and the basal transcriptional machinery, thus modulating the transcription of genes that take part in endothelial differentiation. EDF1 binds calmodulin through its IQ domain and controls nitric oxide synthase activity via calmodulin sequestration in the cytoplasm. EDF1 is localized in adult liver, heart, adipose tissues, intestine and pancreas.
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Synonyms
EDF-1, MBF1, Multiprotein-bridging factor 1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze thaw cycles.
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Amino Acid Sequence
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV LGKIERAIGL KLRGKDIGKP IEKGPRAKLE 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 :
Noggin MouseDescription:
Noggin Mouse Recombinant
Noggin, SYM1, SYNS1, NOG.
Product # :
CYT-600Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Noggin Mouse Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked protein consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.4 kDa (each chain 23.2 kDa).
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% acetonitrile, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by inhibiting BMP-4-induced alkaline phosphatase production of murine ATDC5 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg in the presence of 5ng/ml BMP-4.More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
Noggin, SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYD
PGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKG
LEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRF
WPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGQR
CGWIPIQYPIISECKCSC.
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 :
BRD3 HumanDescription:
Bromodomain Containing 3 Human Recombinant
ORFX, RING3L, Bromodomain-containing protein 3, RING3-like protein, KIAA0043, RING3L.
Product # :
PRO-2143Price :
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Description
BRD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-416 a.a) and having a molecular mass of 48.1kDa.BRD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BRD3 protein solution (0.5mg/ml) containing PBS buffer (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Bromodomain Containing 3 (BRD3) was classified based on its homology to the gene encoding the RING3 protein, which is a serine/threonine kinase. The BRD3 protein localizes to 9q34, a region which contains a number of major histocompatibility complex (MHC) genes. The function of the BRD3 protein is unknown.
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Synonyms
ORFX, RING3L, Bromodomain-containing protein 3, RING3-like protein, KIAA0043, RING3L.
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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 MGSMSTATTV APAGIPATPG PVNPPPPEVS NPSKPGRKTN QLQYMQNVVV KTLWKHQFAW PFYQPVDAIK LNLPDYHKII KNPMDMGTIK KRLENNYYWS ASECMQDFNT MFTNCYIYNK PTDDIVLMAQ ALEKIFLQKV AQMPQEEVEL LPPAPKGKGR KPAAGAQSAG TQQVAAVSSV SPATPFQSVP PTVSQTPVIA ATPVPTITAN VTSVPVPPAA APPPPATPIV PVVPPTPPVV KKKGVKRKAD TTTPTTSAIT ASRSESPPPL SDPKQAKVVA RRESGGRPIK PPKKDLEDGE VPQHAGKKGK LSEHLRYCDS ILREMLSKKH AAYAWPFYKP VDAEALELHD YHDIIKHPMD LSTVKRKMDG REYPDAQGFA ADVRLMFSNC YKYNPPDHEV VAMARKLQDV FEMRFAKMP.
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 :
CAMLG HumanDescription:
Calcium Modulating Ligand Human Recombinant
Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.
Product # :
PRO-1612Price :
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Description
CAMLG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189) and having a molecular mass of 23.2kDa.CAMLG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CAMLG solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CAMLG binds to cyclophilin B and operates downstream of the TCR and upstream of calcineurin by causing an influx of calcium. CAMLG is an essential membrane protein that takes part in the calcium signal transduction pathway, connecting cyclophilin B to calcium signaling.
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Synonyms
Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.
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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 MGSMESMAVA TDGGERPGVP AGSGLSASQR RAELRRRKLL MNSEQRINRI MGFHRPGSGA EEESQTKSKQ QDSDKLNSLS VPSVSKRVVL GDSVSTGTTD QQGGVAEVKG TQLGDKLDSF IKPPECSSDV NLELRQRNRG DLTADSVQRG SRHGLEQYLS RFEEAMKLRK QLISEKPSQE DGNTTEEFDS FR
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 :
CETN3 HumanDescription:
Centrin-3 Human Recombinant
CEN3, CEN-3, CETN-3.
Product # :
PRO-533Price :
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Description
CETN3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.7 kDa. CETN3 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CETN3 Human 0.5mg/ml solution contains 20mM Trsi HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.
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Synonyms
CEN3, CEN-3, CETN-3.
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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 MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD VKKADVLKIL
KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI
AIMTGDI.
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 :
COTL1 HumanDescription:
Coactosin-Like 1 Human Recombinant
Coactosin-like protein, COTL1, CLP, FLJ43657, MGC19733.
Product # :
PRO-064Price :
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Description
COTL1 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 162 amino acids (1-142 a.a.) and having a molecular mass of 18.1kDa. The COTL1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The COTL1 solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Coactosin-like protein (COTL1) is one of the numerous actin-binding proteins which regulate the actin cytoskeleton. COTL1 binds F-actin, it also interacts with 5-lipoxygenase, which is the first committed enzyme in leukotriene biosynthesis. COTL1 binds to F-actin in a calcium-independent way and has no direct effect on actin depolymerization.
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Synonyms
Coactosin-like protein, COTL1, CLP, FLJ43657, MGC19733.
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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 MATKIDKEAC RAAYNLVRDD GSAVIWVTFK YDGSTIVPGE QGAEYQHFIQ QCTDDVRLFA FVRFTTGDAM SKRSKFALIT WIGENVSGLQ RAKTGTDKTL VKEVVQNFAK EFVISDRKEL EEDFIKSELK KAGGANYDAQ TE.
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 :
BD 2 MouseDescription:
Beta Defensin-2 Mouse Recombinant
Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.
Product # :
CYT-035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Beta Defensin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5.5kDa. The BD-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse BD-2 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.More Info
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Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
BBeta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.
Variation in human Beta Defensin-1 contributes to asthma diagnosis, with apparent gender-specific effects. Human Beta Defensin-3 is a dimer, while Human BD-1 and Human BD-2 are monomeric. The expression of Human BD1 is correlated with induction profiles in gingival keratinocytes.
The level of expression of human DEFB1 mRNA is lower than that of human BD3 and human BD-2 in reconstructed epidermis.
Human BD1 is down-regulated in human prostatic and renal carcinomas. -
Synonyms
Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Beta Defensin-2 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-2 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.
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Background
What is the molecular weight/Mw of BD2 Protein?
BD2 Protein has a total Mw of 5.5kDa.
What is the source or expression system of BD2 Protein?
Escherichia Coli.
What is the Purity of BD2 Protein?
BD2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD2 Protein?
Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.
What is the amino acid sequence of BD2 Protein?
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.
What applications can BD2 Protein be used in?
BD2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD2 Protein?
The endotoxin level is minimal, BD2 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.
- View Data Sheet
Name :
CD105 (27-581) MouseDescription:
Endoglin (27-581) Mouse Recombinant
Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.
Product # :
CYT-972Price :
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Shipped with Ice Packs
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Description
Endoglin Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-581 a.a.) and having a molecular mass of 60.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).Endoglin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Endoglin protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities. -
Synonyms
Endoglin, Cell surface MJ7/18 antigen, CD105, Eng, Edg.
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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
ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH
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Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 60.9kDa.
What is the source or expression system of CD105 Protein?
Sf9, Baculovirus cells.
What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.
What is the amino acid sequence of CD105 Protein?
ERVGCDLQPV DPTRGEVTFT TSQVSEGCVA QAANAVREVH VLFLDFPGML SHLELTLQAS KQNGTETQEV FLVLVSNKNV FVKFQAPEIP LHLAYDSSLV IFQGQPRVNI TVLPSLTSRK QILDWAATKG AITSIAALDD PQSIVLQLGQ DPKAPFLCLP EAHKDMGATL EWQPRAQTPV QSCRLEGVSG HKEAYILRIL PGSEAGPRTV TVMMELSCTS GDAILILHGP PYVSWFIDIN HSMQILTTGE YSVKIFPGSK VKGVELPDTP QGLIAEARKL NASIVTSFVE LPLVSNVSLR ASSCGGVFQT TPAPVVTTPP KDTCSPVLLM SLIQPKCGNQ VMTLALNKKH VQTLQCTITG LTFWDSSCQA EDTDDHLVLS SAYSSCGMKV TAHVVSNEVI ISFPSGSPPL RKKVQCIDMD SLSFQLGLYL SPHFLQASNT IELGQQAFVQ VSVSPLTSEV TVQLDSCHLD LGPEGDMVEL IQSRTAKGSC VTLLSPSPEG DPRFSFLLRV YMVPTPTAGT LSCNLALRPS TLSQEVYKTV SMRLNIVSPD LSGKGLEHHH HHH
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Fibronectin RecombinantDescription:
Fibronectin Human Recombinant
Product # :
PRO-2621Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Fibronectin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 574 amino acids and having a molecular mass of 62.6kDa. The Fibronectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, with 5 % Trehalose and 0.02 % Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Was measured by its ability to support cell attachment and spreading when used as a substratum for cell culture. The recommended concentration in this application for this effect is typically 1-5 μg/cm2. Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/ml. Optimal concentrations will need to be determined for individual user applications.
More Info
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Introduction
Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Fibronectin 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 :
IP10 Guinea PigDescription:
IP-10 (CXCL10) Guinea Pig Recombinant
CXCL10, CRG-2.
Product # :
CHM-046Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
IP10 Guinea Pig Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a total molecular mass of 8.7kDa.The IP10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM Sodium Phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
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Synonyms
CXCL10, CRG-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IP10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IP10 Human 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 IP10 in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
IPHSRTIRCT CIETSTQPVN PKSFKKLEII PASQSCPRVE IIATMKMNGE KRCLDPESKV IKNLLKAVRK ERSKRS
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 :
CoV-2 Spike (318-542)Description:
Coronavirus 2019 Spike Receptor Binding Domain (318-542 a.a.) Recombinant
Product # :
SARS-057Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Coronavirus 2019 Spike Receptor Binding Domain (318-542 aa) having a Mw of 25.7kDa was purified from E. coli.The CoV-2 Spike is fused to a 6xHis tag at its C terminal and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
CoV-2 Spike protein solution contains PBS and 25mM K2CO3.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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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
HMRVQPTESI VRFPNITNLC PFGEVFNATR FASVYAWNRK RISNCVADYS VLYNSASFS TFKCYGVSPT KLNDLCFTNV YADSFVIRGD EVRQIAPGQT GKIADYNYKL PDDFTGCVI AWNSNNLDSKV GGNYNYLYRL FRKSNLKPFE RDISTEIYQA GSTPCNGVEG FNCYFPLQSY GFQPTNGVGY QPYRVVVLSF ELLHAPATVC GPKKSTNLVK NKCVNFNLE
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Applications
ELISA, Western blot and lateral flow immunoassay.
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 :
Adiponectin Human (72-244)Description:
Adiponectin (72-244) Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-1231Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The Adiponectin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 24kDa protein containing 173 amino acid residues of the Acrp30 Human, 72-244 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Adiponectin 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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN
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Background
Adiponectin is a protein produced and secreted by adipose tissue. Adiponectin takes part in regulating glucose levels as well as fatty acid breakdown.
Adiponectin ‘s Functions:
Anti-Inflammatory Effects - Adiponectin has anti-inflammatory properties that helps mitigate chronic inflammation.
Regulation of Glucose and Lipid Metabolism - Adiponectin Enhances insulin sensitivity, helping in regulation of blood sugar levels and also promotes fatty acid oxidation, which helps reduce fat accumulation.
Cardiovascular Health - It may influence vascular health and is associated with a lower risk of cardiovascular diseases.
Levels and Health Implications:
Normal Levels - usually, higher levels of adiponectin are associated with a lower risk of metabolic syndrome, cardiovascular diseases and type 2 diabetes.
Low Levels - Reduced adiponectin levels are often linked with obesity, insulin resistance, and other metabolic disorders.
Factors Influencing on the Adiponectin Levels:
Weight - High body fat (especially visceral fat) can lower adiponectin levels.
Diet and Exercise - Regular physical activity and a healthy diet can increase adiponectin levels.
Genetics - Genetic factors might also be an influence on an individual adiponectin level.
Adiponectin is an important component in metabolic health, therefore continuing the research of its functions and regulation keeps advance our understanding of its role in diseases like diabetes and cardiovascular conditions.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24kDa.What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTINProtein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN.
What applications can ADIPONECTIN Protein be used in ?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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.
- View Data Sheet
Name :
HEV ORF3Description:
Hepatitis E Virus ORF3 Recombinant
Product # :
HEV-273Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- formulation
- purity
- More Info
Description
The e.coli derived HEV protein is fused with beta-galactosidase at the N-Terminus and contains the HEV immunodominant ORF3 92-123 a.a.
Formulation
20mM Tris-HCl, pH-8, 10mM B-ME and 8M urea.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.
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Stability
HEV ORF3 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Specificity
Immunoreactive with sera HEV-infected individuals.
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Purification Method
HEV ORF3 protein was purified by proprietary chromatographic technique.
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.