Search: 357 results found for "pih1 domain containing"

Description:

Hemoglobin-Zeta Mouse Recombinant

Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.

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PRO-2517

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Description

HBZ Mouse Recombinant 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 18.3kDa.HBZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HBZ protein solution (0.25mg/ml) containing 20mM MES(pH6.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.
Synonyms
Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLMKNERAI IMSMWEKMAA QAEPIGTETL ERLFCSYPQT KTYFPHFDLH HGSQQLRAHG FKIMTAVGDA VKSIDNLSSA LTKLSELHAY ILRVDPVNFK LLSHCLLVTM AARFPADFTP EVHEAWDKFM SILSSILTEK YR.

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.

Description:

SARS MERS Spike Receptor Binding Domain Recombinant, Active

Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein

Product # :

SARS-060

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Description

SARS MERS RBD Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 258 amino acids (358-606 aa) and having a molecular mass of 28.2kDa. SARS MERS RBD is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The SARS MERS RBD solution (0.5mg/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 binding ability in a functional ELISA with Human DPPIV/CD26 (CAT# enz-1187).

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Synonyms
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPSGVYSVS SFEAKPSGSV VEQAEGVECD FSPLLSGTPP QVYNFKRLVF TNCNYNLTKL LSLFSVNDFT CSQISPAAIA SNCYSSLILD YFSYPLSMKS DLSVSSAGPI SQFNYKQSFS NPTCLILATV PHNLTTITKP LKYSYINKCS RLLSDDRTEV PQLVNANQYS PCVSIVPSTV WEDGDYYRKQ LSPLEGGGWL VASGSTVAMT EQLQMGFGIT VQYGTDTNSV CPKLEFANDT KIASQLGNCV EYHHHHHH.
Background
The severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) have posed significant global health threats in recent years. Central to their pathogenesis is the interaction between the viral spike proteins and host cell receptors. This research aims to investigate the receptor binding domain (RBD) of SARS and MERS spike proteins and its implications for viral entry and the development of therapeutic interventions. Understanding the molecular mechanisms underlying viral-host interactions can pave the way for targeted therapeutic strategies against these deadly coronaviruses.
Structure and Function of SARS and MERS Spike RBD:
The spike proteins of SARS-CoV and MERS-CoV are critical for viral entry into host cells. These proteins consist of two subunits: S1, responsible for receptor binding, and S2, involved in membrane fusion. The receptor binding domain (RBD) within the S1 subunit specifically interacts with host cell receptors, enabling viral attachment and entry. The RBDs of SARS and MERS spike proteins exhibit unique structural features and binding affinities for their respective receptors.
Interaction with ACE2 and DPP4 Receptors:
The SARS-CoV spike protein RBD interacts with the angiotensin-converting enzyme 2 (ACE2) receptor, which is abundantly expressed in the respiratory tract. The binding of SARS-CoV RBD to ACE2 facilitates viral entry into host cells. On the other hand, the MERS-CoV spike protein RBD interacts with the dipeptidyl peptidase 4 (DPP4) receptor, predominantly expressed in the lungs and other tissues. The ACE2 and DPP4 receptors play crucial roles in determining the host range and tissue tropism of SARS and MERS coronaviruses.
Implications for Viral Pathogenesis:
The binding of SARS and MERS spike RBDs to their respective receptors triggers conformational changes in the spike protein, leading to membrane fusion and subsequent viral entry. This process is crucial for viral replication and the spread of infection within the host. The specificity and affinity of the RBD-receptor interaction influence viral tropism, tissue damage, and disease severity. Understanding the determinants of RBD-receptor binding can provide insights into viral pathogenesis and potential therapeutic targets.
Development of Therapeutic Interventions:
The RBD of SARS and MERS spike proteins represents a promising target for the development of antiviral therapeutics. Several strategies have been explored, including monoclonal antibodies and small molecule inhibitors, to disrupt the RBD-receptor interaction and inhibit viral entry. These approaches aim to block the binding interface between the spike RBD and the host receptor, thereby preventing viral attachment and entry. Additionally, vaccine development efforts have focused on generating neutralizing antibodies against the RBD to elicit protective immune responses.
Conclusion:
The investigation of the receptor binding domain (RBD) of SARS and MERS spike proteins sheds light on the molecular mechanisms underlying viral entry and pathogenesis. The specific interactions between the spike RBD and host cell receptors play a crucial role in determining viral tropism and tissue damage. Targeting the RBD-receptor interaction holds promise for the development of effective therapeutics against SARS-CoV, MERS-CoV, and potentially other related coronaviruses. Further research and development efforts are needed to exploit the potential of the spike RBD as a therapeutic target and to combat future coronavirus outbreaks.

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.

Description:

Coiled-Coil Domain Containing 90B Human Recombinant

MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.

Product # :

PRO-1478

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Description

CCDC90B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (43-230 a.a) and having a molecular mass of 24.1kDa.CCDC90B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CCDC90B protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Coiled-Coil Domain Containing 90B (CCDC90B) is a member of the CCDC90 family. The CCDC90B protein is distinguished by the presence of a domain of unknown function, DUF1640. The DUF1640 domain is a characteristic of the entire protein with excluding of the first 23 amino acid residues which are a mitochondrial targeting site and the cleaved CCDC90B is expected to be a mitochondrial protein with no transmembrane spans or segments. CCDC90B is predicted to contain at least 3 specific phospohorylation sites.
Synonyms
MDS011, MDS025, CUA003, Coiled-coil domain-containing protein 90B mitochondrial, CCDC90B.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGYDRRPV DITPLEQRKL TFDTHALVQD LETHGFDKTQ AETIVSALTA LSNVSLDTIY KEMVTQAQQE ITVQQLMAHL DAIRKDMVIL EKSEFANLRA ENEKMKIELD QVKQQLMHET SRIRADNKLD INLERSRVTD MFTDQEKQLM ETTTEFTKKD TQTKSIISET SNKIDAEIAS LKTLMESNKL E.

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.

Description:

Starch Binding Domain 1 Human Recombinant

Starch Binding Domain 1, Genethonin 1, GENEX3414, Starch-Binding Domain-Containing Protein 1.

Product # :

PRO-1545

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Description

STBD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (24-358) and having a molecular mass of 39.1kDa.STBD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The STBD1 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.

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Introduction
STBD1 has one carbohydrate binding type-20 (CBM20) domain and has the ability to bind to carbohydrates. STBD1 is highly expressed in cardiac and skeletal muscles.
Synonyms
Starch Binding Domain 1, Genethonin 1, GENEX3414, Starch-Binding Domain-Containing Protein 1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRGGPGDT GKDGDAEQEK DAPLGGAAIP GGHQSGSSGL SPGPSGQELV TKPEHLQESN GHLISKTKDL GKLQAASWRL QNPSREVCDN SREHVPSGQF PDTEAPATSE TSNSRSYSEV SRNESLESPM GEWGFQKGQE ISAKAATCFA EKLPSSNLLK NRAKEEMSLS DLNSQDRVDH EEWEMVPRHS SWGDVGVGGS LKAPVLNLNQ GMDNGRSTLV EARGQQVHGK MERVAVMPAG SQQVSVRFQV HYVTSTDVQF IAVTGDHECL GRWNTYIPLH YNKDGFWSHS IFLPADTVVE WKFVLVENGG VTRWEECSNR FLETGHEDKV VHAWWGIH

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.

Description:

DnaK Substrate Binding Domain E.Coli Recombinant

HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

Product # :

HSP-008

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Description

Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing (385-546 a.a.) 163 amino acids and having a molecular mass of 17.7 kDa.

Source

Escherichia Coli.

Formulation

The protein contains 25mM Tris-HCl, pH7.5, 2mM B-ME and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
Synonyms
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HST.

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.

Description:

SH3-domain GRB2-like 2 Human Recombinant

Endophilin-A1, EEN-B1, Endophilin-1, SH3 domain protein 2A, SH3 domain-containing, GRB2-like protein 2, SH3GL2, CNSA2, SH3D2A, SH3P4.

Product # :

PRO-1083

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Description

SH3GL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-352 a.a) and having a molecular mass of 42.5kDa.SH3GL2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SH3GL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SH3-domain GRB2-like 2 (SH3GL2) is a member of the endophilin family. SH3GL2 contains a BAR domain and a SH3 domain. Members of the BAR domain protein superfamily are crucial elements of cellular traffic. Endophilins have a major function in synaptic vesicle endocytosis (SVE), receptor trafficking and apoptosis, and in other processes which require remodeling of the membrane structure. SH3GL2 is a novel tumor suppressor gene in laryngeal squamous cell carcinoma (LSCC), which induces apoptosis of tumor cells by regulating intra-cellular signal transduction networks. SH3GL2 is implicated in synaptic vesicle endocytosis. SH3GL2 is found in the brain, mainly in frontal cortex, and at high level in the fetal cerebellum.
Synonyms
Endophilin-A1, EEN-B1, Endophilin-1, SH3 domain protein 2A, SH3 domain-containing, GRB2-like protein 2, SH3GL2, CNSA2, SH3D2A, SH3P4.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSVAGL KKQFHKATQK VSEKVGGAEG TKLDDDFKEM ERKVDVTSRA VMEIMTKTIE YLQPNPASRA KLSMINTMSK IRGQEKGPGY PQAEALLAEA MLKFGRELGD DCNFGPALGE VGEAMRELSE VKDSLDIEVK QNFIDPLQNL HDKDLREIQH
HLKKLEGRRL DFDYKKKRQG KIPDEELRQA LEKFDESKEI AESSMFNLLE MDIEQVSQLS ALVQAQLEYH KQAVQILQQV TVRLEERIRQ ASSQPRREYQ PKPRMSLEFP TGDSTQPNGG LSHTGTPKPS GVQMDQPCCR ALYDFEPENE GELGFKEGDI ITLTNQIDEN WYEGMLHGHS
GFFPINYVEI LVALPH.

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.

Description:

Fas-Associated Death Domain, Mouse Anti Human

GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.

Product # :

ANT-344

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
FADD is an adaptor protein that cooperates with a variety of cell surface receptors and mediates cell apoptotic signals. Using its C-terminal death domain, FADD is recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and consequently it take parts in the death signaling initiated by these receptors. FADD interaction with the receptors reviels the N-terminal effector domain of, which allows it to recruit caspase-8, and thus initiate the cysteine protease cascade. Knockout studies in mice furthermore propose the significance of FADD in premature T cell development. FADD plays a role in survival/proliferation and cell cycle development. FADD also takes part in cellular sublocalization, protein phosphorylation, and inhibitory molecules.
Synonyms
GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.
Immunogen
Anti-human FADD mAb is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human FADD amino acids 1-208 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PJ1D2AT.
Applications
FADD antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:1,000~1:2,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:50.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
FADD antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

EGF Like Domain Multiple 6 Mouse Recombinant

Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.

Product # :

CYT-1105

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Description

EGFL6 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 273 amino acids (287-550a.a.) and having a molecular mass of 31.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EGFL6 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

EGFL6 protein solution ( 0.5mg/ml ) contains Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Epidermal Growth Factorlike Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.
Synonyms
Epidermal growth factor-like protein 6, EGF-L6, Egfl6, Maeg.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADLTMKKKVK LKMVTPRPAS TRVPKVNLPY SSEEGVSRGR NYDGEQKKKE EGKRERLEEE
KGEKTLRNEV EQERTLRGDV FSPKVNEAED LDLVYVQRKE LNSKLKHKDL NISVDCSFDL
GVCDWKQDRE DDFDWHPADR DNDVGYYMAV PALAGHKKNI GRLKLLLPNL TPQSNFCLLF
DYRLAGDKVG KLRVFVKNSN NALAWEETKN EDGRWRTGKI QLYQGIDTTK SVIFEAERGK GKTGEIAVDG VLLVSGLCPD DFLSVEGHHH HHH.
Background
Title: EGF-Like Domain Multiple 6 Mouse Recombinant: Insights into its Biological Significance and Potential Applications
Abstract:

EGF-Like Domain Multiple 6 (EGFL6) is a critical protein involved in various biological processes, including development, tissue homeostasis, and cancer progression. This research paper provides a comprehensive analysis of mouse recombinant EGFL6, focusing on its production, characterization, and potential applications in studying its biological functions. The paper highlights the significance of EGFL6 in cellular processes and its role in disease pathogenesis. Furthermore, it discusses ongoing research and potential therapeutic applications of recombinant EGFL6 in cancer and regenerative medicine. The information presented in this paper aims to enhance our understanding of mouse recombinant EGFL6 and its utility as a research tool and a potential therapeutic agent.
Introduction:

EGF-Like Domain Multiple 6 (EGFL6) is a secreted protein that belongs to the epidermal growth factor (EGF) family. Mouse recombinant EGFL6, produced through genetic engineering techniques, provides a valuable tool for investigating its biological functions and potential therapeutic applications.
Production and Characterization:

Recombinant EGFL6 is typically generated using expression systems such as bacteria or mammalian cells. 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 EGFL6.
Biological Significance:

EGFL6 plays a crucial role in diverse cellular processes, including angiogenesis, tissue regeneration, and cell proliferation. It is involved in the modulation of signaling pathways, such as the Wnt/β-catenin pathway, and interacts with extracellular matrix components. Recombinant EGFL6 offers a valuable tool for investigating the molecular mechanisms underlying its biological functions and its involvement in disease pathogenesis.
Role in Cancer:

EGFL6 is implicated in cancer progression and metastasis. It promotes tumor angiogenesis, invasion, and resistance to chemotherapy. Studies utilizing recombinant EGFL6 can contribute to a better understanding of its role in tumor microenvironment remodeling and the development of targeted therapeutic strategies.
Therapeutic Implications:

Given its involvement in various cellular processes and disease pathogenesis, EGFL6 has emerged as a potential therapeutic target. Recombinant EGFL6-based therapies, such as antibody-based approaches or small molecule inhibitors, hold promise for cancer treatment and regenerative medicine. Ongoing research is focused on developing strategies to modulate EGFL6 activity for therapeutic benefit.
Conclusion:

Mouse recombinant EGFL6 serves as a valuable research tool for studying its biological functions and exploring its therapeutic potential. Its production, characterization, and applications in understanding cellular processes and disease pathogenesis contribute to our knowledge of EGFL6 biology and the development of targeted interventions. Continued research and clinical investigations exploring the therapeutic applications of recombinant EGFL6 offer promising avenues for improving outcomes in cancer and regenerative medicine.
What is the molecular weight/Mw of EGFL6 MOUSE Protein?
EGFL6 MOUSE Protein has a total Mw of 31.1kDa.

What is the source or expression system of EGFL6 MOUSE Protein?
Sf9, Insect cells.

What is the Purity of EGFL6 MOUSE Protein?
EGFL6 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EGFL6 MOUSE Protein?
The biological functionality of EGFL6 MOUSE Protein will be determined in the future.

What is the amino acid sequence of EGFL6 MOUSE Protein?
EGFL6 MOUSE Protein is composed from 273 amino acids.

What applications can EGFL6 MOUSE Protein be used in?
EGFL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGFL6 MOUSE Protein?
The endotoxin level is minimal, EGFL6 MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

SCAN domain containing 1 Human Recombinant

RAZ1, SDP1, SCAN domain containing 1, SCAN-related protein RAZ1.

Product # :

PRO-269

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Description

SCAND1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-179 a.a.) and having a molecular mass of 21.2kDa (molecular weight on SDS-PAGE will appear higher).SCAND1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SCAND1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SCAND1 is a part of a family of genes which encode an isolated SCAN domain. SCAN domain containing 1 has one SCAN box domain and has no zinc finger motif, which distinct this protein from almost all other SCAN domain containing proteins. SCAND1 is a nuclear protein that takes a part in the mechanism of transcription regulation. SCAND1 is extensively expressed in high levels in the kidney, thyroid, liver, prostate and testis.
Synonyms
RAZ1, SDP1, SCAN domain containing 1, SCAN-related protein RAZ1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAATEPILAA TGSPAAVPPE KLEGAGSSSA PERNCVGSSL PEASPPAPEP SSPNAAVPEA IPTPRAAASA ALELPLGPAP VSVAPQAEAE ARSTPGPAGS RLGPETFRQR FRQFRYQDAA GPREAFRQLR ELSRQWLRPD IRTKEQIVEM LVQEQLLAIL PEAARARRIR RRTDVRITG

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Description:

Methylmalonyl CoA Epimerase Human Recombinant

GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.

Product # :

ENZ-013

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Description

MCEE produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (37-176a.a.) and having a molecular mass of 17.3kDa.MCEE is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MCEE protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT, 0.1mM PMSF and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
MCEE catalyzes the interconversion of D- and L-methylmalonyl-CoA throughout the degradation of branched chain amino acids, odd chain-length fatty acids, and other metabolites. MCEE protein deficiency is an autosomal recessive inborn error of amino acid metabolism, involving valine, threonine, isoleucine and methionine. This organic aciduria can appear in the neonatal period with life-threatening metabolic acidosis, hyperammonemia, feeding difficulties, pancytopenia and coma.
Synonyms
GLOD2, Methylmalonyl CoA Epimerase, Glyoxalase Domain Containing 2, DL-methylmalonyl-CoA Racemase.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQVTGSVWNL GRLNHVAIAV PDLEKAAAFY KNILGAQVSE AVPLPEHGVS VVFVNLGNTK MELLHPLGRD SPIAGFLQKN KAGGMHHICI EVDNINAAVM DLKKKKIRSL SEEVKIGAHG KPVIFLHPKD CGGVLVELEQ A

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.

Description:

Protein Phosphatase-1 Regulatory Subunit-14A, Mouse Anti Human

Protein phosphatase 1 regulatory subunit 14A, 17 kDa PKC-potentiated inhibitory protein of PP1, CPI17, CPI-17, PPP1INL, PPP1R14A.

Product # :

ANT-381

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
PPP1R14A is a phosphorylation-dependent inhibitor of smooth muscle myosin phosphatase. Inhibition of PPP1R14A results to increased myosin phosphorylation and enhances smooth muscle contraction in the absence of increased intracellular Ca(2+) concentration. Myosin phosphatase can reverse MYL (myosin light chain) phosphorylation to induce a state of relaxation. However, during agonist-induced contraction at constant Ca2+ concurrent inhibition of myosin phosphatase leads to increases in MYL phosphorylation and tension. These calcium-independent increases in myosin phosphorylation and tension are termed calcium sensitization. Human pregnancy is characterized by the increases of PKN1 expression and CPI-17 phosphorylation in the myometrium. PPP1R14A is mapped to chromosome 19q13.13-q13.2. PPP1R14A binds directly to protein kinase C and casein kinase I. PPP1R14A siRNA decreased the level of merlin phosphorylation and consequently Ras and ERK activity in human tumor cell lines. PKC/CPI-17 medi
Synonyms
Protein phosphatase 1 regulatory subunit 14A, 17 kDa PKC-potentiated inhibitory protein of PP1, CPI17, CPI-17, PPP1INL, PPP1R14A.
Immunogen
Anti-human PPP1R14A mAb is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PPP1R14A amino acids 1-147 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
Clone
P4H10AT.
Applications
PPP1R14A antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
PPP1R14A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Abhydrolase Domain Containing 12B Human Recombinant

BEM46L3, c14_5314, Abhydrolase domain-containing protein 12B, ABHD12B, C14orf29.

Product # :

PRO-1998

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Description

ABHD12B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-255a.a) and having a molecular mass of 31.0kDa. ABHD12B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ABHD12B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Abhydrolase Domain Containing 12B, also known as ABHD12B is a part of the serine esterase family. ABHD12B is a protein coding gene.
Synonyms
BEM46L3, c14_5314, Abhydrolase domain-containing protein 12B, ABHD12B, C14orf29.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLGIWHT VPSCRGEDAK GKDCCWYEAA LRDGNPIIVY LHGSAEHRAA SHRLKLVKVL SDGGFHVLSV DYRGFGDSTG KPTEEGLTTD AICVYEWTKA RSGITPVCLW GHSLGTGVAT NAAKVLEEKG CPVDAIVLEA PFTNMWVASI NYPLLKIYRN IPGFLRTLMD ALRKDKIIFP NDENVKFLSS PLLILHGEDD RTVPLEYGKK LYEIARNAYR NKERVKMVIF PPGFQHNLLC KSPTLLITVR DFLSKQWS.

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.

Description:

Heat shock 70kDa protein 5 Human Recombinant, Hi-5

78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.

Product # :

HSP-037

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Description

HSPA5 produced in Hi-5 cells is a single, glycosylated polypeptide chain containing 640 amino acids (20-650 a.a.) and having a molecular mass of 71kDa. HSPA5 is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Hi-5 Cells.

Formulation

The HSPA5 protein solution (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 200mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Binding immunoglobulin protein (BiP or HSPA5) is a member of the family of ~70kDa heat shock proteins (HSP 70). HSPA5 is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. HSPA5 is crucial for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis.
Synonyms
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MEEDKKEDVG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKFLPFK VVEKKTKPYI QVDIGGGQTK TFAPEEISAM VLTKMKETAE AYLGKKVTHA VVTVPAYFND AQRQATKDAG TIAGLNVMRI INEPTAAAIA YGLDKREGEK NILVFDLGGG TFDVSLLTID NGVFEVVATN GDTHLGGEDF DQRVMEHFIK LYKKKTGKDV RKDNRAVQKL RREVEKAKRA LSSQHQARIE IESFYEGEDF SETLTRAKFE ELNMDLFRST MKPVQKVLED SDLKKSDIDE IVLVGGSTRI PKIQQLVKEF FNGKEPSRGI NPDEAVAYGA AVQAGVLSGD QDTGDLVLLD VCPLTLGIET VGGVMTKLIP RNTVVPTKKS QIFSTASDNQ PTVTIKVYEG ERPLTKDNHL LGTFDLTGIP PAPRGVPQIE VTFEIDVNGI LRVTAEDKGT GNKNKITITN DQNRLTPEEI ERMVNDAEKF AEEDKKLKER IDTRNELESY AYSLKNQIGD KEKLGGKLSS EDKETMEKAV EEKIEWLESH QDADIEDFKA KKKELEEIVQ PIISKLYGSA GPPPTGEEDT AELEHHHHHH.

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.

Description:

Ras association domain-containing protein 1 Human Recombinant

123F2, NORE2A, RASSF1, RDA32, REH3P21, Ras association domain-containing protein 1.

Product # :

PRO-1288

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Description

RASSF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-340 a.a.) and having a molecular mass of 42.9kDa. RASSF1A is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RASSF1A protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
RASSF1A protein is a potential tumor suppressor like the RAS effector proteins. Presence or absence expression of this gene has been related with the pathogenesis of a variety of cancers, which suggests the tumor suppressor function of this RASSF1A gene. The inactivation of RASSF1A was found to be associated with the hypermethylation of its CpG-island promoter region. RASSF1A required for death receptor-dependent apoptosis.
Synonyms
123F2, NORE2A, RASSF1, RDA32, REH3P21, Ras association domain-containing protein 1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSGE PELIELRELA PAGRAGKGRT RLERANALRI ARGTACNPTR QLVPGRGHRF QPAGPATHTW CDLCGDFIWG VVRKGLQCAH CKFTCHYRCR ALVCLDCCGP RDLGWEPAVE RDTNVDEPVE WETPDLSQAE IEQKIKEYNA QINSNLFMSL NKDGSYTGFI KVQLKLVRPV SVPSSKKPPS LQDARRGPGR GTSVRRRTSF YLPKDAVKHL HVLSRTRARE VIEALLRKFL VVDDPRKFAL FERAERHGQV YLRKLLDDEQ PLRLRLLAGP SDKALSFVLK ENDSGEVNWD AFSMPELHNF LRILQREEEE HLRQILQKYS YCRQKIQEAL HACPLG.

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.

Description:

Interleukin-36 Alpha Mouse Recombinant, His Tag

Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.

Product # :

CYT-905

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Description

IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-160 a.a) and having a molecular mass of 20.4kDa. IL36A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL36A protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Human IL-36a belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36a is an 18-22kDa, 158aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential from N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Human IL-36a (aa 6-158) shares 57-68% aa sequence homology with mouse, rabbit, equine and bovine IL-36a and 27-57% aa sequence homology with other new IL-1 family members. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.
Synonyms
Interleukin-36 alpha, FIL1 epsilon, Interleukin-1 epsilon, IL-1 epsilon, Interleukin-1 family member 6, IL-1F6, Interleukin-1 homolog 1, IL-1H1, Il36a, Fil1e, Il1e, Il1f6, Il1h1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNKEKEL RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH.

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.

Description:

WAP Four-Disulfide Core Domain 12 Human Recombinant

WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.

Product # :

PRO-1830

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Description

WFDC12 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (24-111) and having a molecular mass of 12.1 kDa. WFDC12 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The WFDC12 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
WFDC12 belongs to the WFDC (WAP-type four-disulfide core) domain family. The WAP signature motif or WFDC domain has four disulfide bonds created by eight cysteines at the core of the protein, which operates as a protease inhibitor.
Synonyms
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVKEGIEK AGVCPADNVR CFKSDPPQCH TDQDCLGERK CCYLHCGFKC VIPVKELEEG GNKDEDVSRP YPEPGWEAKC PGSSSTRCPQ K

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.

Description:

3-Hydroxy-3-Methylglutaryl-CoA Synthase 1 Human Recombinant

3-Hydroxy-3-Methylglutaryl-CoA Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl-Coenzyme A Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl Coenzyme A (HMG-CoA) Synthase, EC 2.3.3.10, HMGCS, Hydroxymethylglutaryl-CoA Synthase, Cytoplasmic, 3-Hydroxy-3-Methylglutaryl Coenzyme A Synthase, HMG-CoA Synthase.

Product # :

ENZ-870

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Description

HMGCS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 543 amino acids (1-520 a.a) and having a molecular mass of 59.7kDa.HMGCS1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HMGCS1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
3-Hydroxy-3-Methylglutaryl-CoA Synthase 1, also known as HMGCS1 is a member of the Belongs to the HMG-CoA synthase family. HMGCS1 condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.
Synonyms
3-Hydroxy-3-Methylglutaryl-CoA Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl-Coenzyme A Synthase 1 (Soluble), 3-Hydroxy-3-Methylglutaryl Coenzyme A (HMG-CoA) Synthase, EC 2.3.3.10, HMGCS, Hydroxymethylglutaryl-CoA Synthase, Cytoplasmic, 3-Hydroxy-3-Methylglutaryl Coenzyme A Synthase, HMG-CoA Synthase.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPGSLPL NAEACWPKDV GIVALEIYFP SQYVDQAELE KYDGVDAGKY TIGLGQAKMG FCTDREDINS LCMTVVQNLM ERNNLSYDCI GRLEVGTETI IDKSKSVKTN LMQLFEESGN TDIEGIDTTN ACYGGTAAVF NAVNWIESSS WDGRYALVVA GDIAVYATGN ARPTGGVGAV ALLIGPNAPL IFERGLRGTH MQHAYDFYKP DMLSEYPIVD GKLSIQCYLS ALDRCYSVYC KKIHAQWQKE GNDKDFTLND FGFMIFHSPY CKLVQKSLAR MLLNDFLNDQ NRDKNSIYSG LEAFGDVKLE DTYFDRDVEK AFMKASSELF SQKTKASLLV SNQNGNMYTS SVYGSLASVL AQYSPQQLAG KRIGVFSYGS GLAATLYSLK VTQDATPGSA LDKITASLCD LKSRLDSRTG VAPDVFAENM KLREDTHHLV NYIPQGSIDS LFEGTWYLVR VDEKHRRTYA RRPTPNDDTL DEGVGLVHSN IATEHIPSPA KKVPRLPATA AEPEAAVISN GEH

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.

Description:

Ras association domain-containing protein 1, Mouse Anti Human

Ras association domain-containing protein 1, 123F2, RDA32, NORE2A, RASSF1A, REH3P21, RASSF1.

Product # :

ANT-400

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
RASSF1A is a protein similar to the RAS effector proteins. Loss or altered expression of the RASSF1A gene has been linked to the pathogenesis of a variety of cancers, which suggests the tumor suppressor function of the RASSF1A gene. The inactivation of the RASSF1A gene was found to be interconnected with the hypermethylation of its CpG-island promoter region. The RASSF1A protein was found to interact with DNA repair protein XPA. RASSF1A was also shown to inhibit the accumulation of cyclin D1, and thus induce cell cycle arrest.
Synonyms
Ras association domain-containing protein 1, 123F2, RDA32, NORE2A, RASSF1A, REH3P21, RASSF1.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human RASSF1A mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human RASSF1A amino acids 1-340 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P3F3AT.
Applications
RASSF1A antibody has been tested by ELISA, Western blot and immunocytochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:2,000. Recommended starting dilution is 1:1,000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
RASSF1A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Interleukin-1 alpha Human Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-253

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source
formulation
purity
biological activity
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Description

Interleukin-1 alpha Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids and having a molecular mass of 18022 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 25mM Tris-HCl, pH 8.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 10⁹ IU/mg.

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Introduction
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.
Background
What is the molecular weight/Mw of IL1A HUMAN Protein?
IL1A HUMAN Protein has a total Mw of 18kDa.

What is the source or expression system of IL1A HUMAN Protein?
Escherichia Coli.

What is the Purity of IL1A HUMAN Protein?
IL1A HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.

What is the amino acid sequence of IL1A HUMAN Protein?
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.

What applications can IL1A HUMAN Protein be used in?
IL1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A HUMAN Protein?
The endotoxin level is minimal, IL1A HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.13 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.

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

Description:

Prostaglandin Reductase 2 Human Recombinant

Prostaglandin reductase 2, PRG-2, 15-oxoprostaglandin 13-reductase, Zinc-binding alcohol dehydrogenase domain-containing protein 1, PTGR2, ZADH1, PGR2.

Product # :

ENZ-601

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Description

PTGR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (1-351) and having a molecular mass of 41.1kDa.PTGR2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PTGR2 solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 50mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Prostaglandin Reductase 2 (PTGR2) is a member of the medium-chain dehydrogenase/reductase superfamily. PTGR2 is an enzyme involved in the metabolism of prostaglandins. PTGR2 catalyzes an NADPH-dependent reduction of the conjugated alpha, beta-unsaturated double bond of 15-keto-PGE(2), which is a fundamental step in terminal inactivation of prostaglandins and suppression of PPARgamma-mediated adipocyte differentiation. PTGR2 may also be involved in controlling activation of the peroxisome proliferator-activated receptor.
Synonyms
Prostaglandin reductase 2, PRG-2, 15-oxoprostaglandin 13-reductase, Zinc-binding alcohol dehydrogenase domain-containing protein 1, PTGR2, ZADH1, PGR2.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIVQRV VLNSRPGKNG NPVAENFRME EVYLPDNINE GQVQVRTLYL SVDPYMRCRM NEDTGTDYIT PWQLSQVVDG GGIGIIEESK HTNLTKGDFV TSFYWPWQTK VILDGNSLEK VDPQLVDGHL SYFLGAIGMP GLTSLIGIQE KGHITAGSNK
TMVVSGAAGA CGSVAGQIGH FLGCSRVVGI CGTHEKCILL TSELGFDAAI NYKKDNVAEQ LRESCPAGVD VYFDNVGGNI SDTVISQMNE NSHIILCGQI SQYNKDVPYP PPLSPAIEAI QKERNITRER FLVLNYKDKF EPGILQLSQW FKEGKLKIKE TVINGLENMG AAFQSMMTGG
NIGKQIVCIS EEISL.

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.

Description:

Hydroxylysine Kinase Human Recombinant

Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 1.

Product # :

PKA-064

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Shipped with Ice Packs

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Description

HYKK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.3kDa.HYKK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

HYKK solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 40% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Hydroxylysine Kinase, also known as HYKK, is a Protein Coding gene. HYKK which is a part of the aminoglycoside phosphotransferase family catalyzes the GTPdependent phosphorylation of 5-hydroxy-L-lysine.
Synonyms
Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSGNYQ QSEALSKPTF SEEQASALVE SVFGLKVSKV RPLPSYDDQN FHVYVSKTKD GPTEYVLKIS NTKASKNPDL IEVQNHIIMF LKAAGFPTAS VCHTKGDNTA SLVSVDSGSE IKSYLVRLLT YLPGRPIAEL PVSPQLLYEI GKLAAKLDKT LQRFHHPKLS SLHRENFIWN LKNVPLLEKY LYALGQNRNR EIVEHVIHLF KEEVMTKLSH FRECINHGDL NDHNILIESS KSASGNAEYQ VSGILDFGDM SYGYYVFEVA ITIMYMMIES KSPIQVGGHV LAGFESITPL TAVEKGALFL LVCSRFCQSL VMAAYSCQLY PENKDYLMVT AKTGWKHLQQ MFDMGQKAVE EIWFETAKSY ESGISM.

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.

Description:

TROVE Domain Family Member 2 Human Recombinant

60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

Product # :

PRO-329

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Description

RO-60 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 60kDa. RO60 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein solution contains 6M Urea, 500mM NaCl, 500mM imidazole and 10mM Tris pH-6.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Physical Appearance
Sterile Filtered clear solution.
Stability
RO-60 although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent 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.

Description:

EGF Like Domain Multiple 6 Human Recombinant

EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.

Product # :

CYT-974

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Shipped at Room temp

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Description

EGF Like Domain Multiple 6 Human Recombinant produced in HEK cells is a polypeptide chain starting at amino acid Asn at position 22 to amino acid Arg at position 363, fused to an FC, 6 x His-tag at C-terminus, containing a total of 348 amino acids and having a predicted molecular mass of 40-55kDa. The EGFL6 is purified by proprietary chromatographic techniques.

Source

HEK (Human embryonic kidney cells).

Formulation

The EGFL6 protein was lyophilized from a 0.2µm filtered solution in 20mM MES and 500mM NaCl, pH 6.0 with 5% Trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

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Introduction
Epidermal Growth Factorlike Domain Multiple 6 (EGFL6) belongs to the EGF repeat superfamily of proteins, whose members are involved in the regulation of cell cycle, proliferation, and developmental processes. EGFL6 gene product contains a signal peptide, suggesting that EGFL6 is secreted; an EGF repeat region consisting of four complete EGF-like repeats and 1 partial EGF-like repeat, 3 of which have a calcium-binding consensus sequence; an arg-gly-asp integrin association motif; and a MAM domain, which is assumed to have an adhesive function. Within shared regions, human EGFL6 shares 75% and 78% amino acid sequence identity with the mouse and rat orthologs, respectively. EGFL6 is expressed in various fetal tissues during early development such as the lung, heart, liver, spleen, cochlea and the placenta, as well as meningioma tumors.
Synonyms
EGF Like Domain Multiple 6, MAM and EGF Domains-Containing Gene Protein, MAM and EGF Domain Containing, EGF-Like Protein 6, MAEG, EGF Repeat-Containing Protein 6, W80, EGFL6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EGFL6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGFL6 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized EGFL6 in sterile PBS at 500µg/ml, which can then be further diluted to other aqueous solutions.
Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGFL6 HUMAN Protein?
EGFL6 HUMAN Protein has a total Mw of 40-55kDa.

What is the source or expression system of EGFL6 HUMAN Protein?
HEK (Human embryonic kidney cells).

What is the Purity of EGFL6 HUMAN Protein?
EGFL6 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EGFL6 HUMAN Protein?
EGFL6 activity is determined by its ability of the immobilized protein to support the adhesion of NIH-3T3 mouse embryonic fibroblast cells. The expected ED50 for this effect is 1-5 μg/ml.

What is the amino acid sequence of EGFL6 HUMAN Protein?
EGFL6 HUMAN Protein is composed from 348 amino acids.

What applications can EGFL6 HUMAN Protein be used in?
EGFL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGFL6 HUMAN Protein?
The endotoxin level is minimal, EGFL6 HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-36 Alpha Mouse Recombinant

Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

Product # :

CYT-162

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Shipping Method :

Shipped at Room temp

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Description

IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 21.0kDa.The IL36A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA to bind recombinant mouse IL-1 Rrp2.

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Introduction
Murine IL-36a belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. Murine IL-36a is a 160 amino acid intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Mouse to human, full length IL-36a/IL-1F6 shares 54% aa sequence homology. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.
Synonyms
Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36A Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL36A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH

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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